Does Science Need a Radical Shift to Explain Life’s Origin?

Imagine you’ve been handed the keys to a time machine. With a mixture of excitement, you step inside, set the dial to “Just before the origin of life on Earth,” and press the button. As the door creaks open, you brace yourself for what lies beyond. What would you see in this lifeless world?

Here is what we suspect, and what we are told: a planet shaped by barren rock, vast oceans, and a dense atmosphere of swirling gases. Volcanic eruptions carve the landscape, saturating the air with heat and chemicals, while relentless forces sculpt an unforgiving surface. Yet, in the midst of this chaotic planet, a tiny, improbable oasis formed—an unlikely “Eden” in which life is believed to have emerged. From lifeless matter, a mysterious transformation known as chemical evolution unfolded and life blinked into existence.

If you start with a naturalistic view of the universe, then you are led to believe that the emergence of life must have happened without any blueprint or guiding hand. The natural world is viewed as a self-explanatory system, where all events result from nature’s own mechanisms that are themselves without mindful or transcendent explanations. It’s not just that every phenomenon can be explained by natural mechanisms; these mechanisms are also fully capable of explaining themselves without any need for higher, non-material explanations.

*The following is an excerpt from our upcoming book. Details will soon be released. This is part one of four in the book.

Exploring the Great Divide: Life and Non-life

One of the initial challenges in discussing the origin of life is pinpointing the moment when non-living chemical systems transition into living organisms. It’s tough to define what constitutes biological life because there isn’t a universally accepted definition. Common characteristics of life include the ability to reproduce, evolve, maintain metabolism, and process genetic information, but the lack of a clear definition makes conversations about the origin of life more complex.

In school, I was led to believe that the transition from non-life to life was straightforward, with the earliest forms of life being very simple and barely distinguishable from non-living matter. However, this oversimplifies the complexity of a “simple” biological structure. The reality is that even the earliest forms of life exhibited a remarkable degree of complexity. Geneticist Michael Denton paints a vivid picture of the divide between life and non-life, declaring:

“it represents the most dramatic and fundamental of all the discontinuities of nature. Between a living cell and the most highly ordered non-biological systems, such as a crystal or a snowflake, there is a chasm as vast and absolute as it is possible to conceive.”¹

Denton illustrates this by pointing to the smallest bacterial cells, which weigh less than a trillionth of a gram, yet are akin to a “veritable micro-miniaturised factory containing thousands of exquisitely designed pieces of intricate molecular machinery, made up altogether of 100 thousand million atoms, far more complicated than any machine built by man and absolutely without parallel in the non-living world.”²

It’s pretty fascinating that research in molecular biology has uncovered a fascinating truth: the inner workings of cells across all life forms are strikingly consistent. At the heart of it all are DNA, RNA, and proteins—the molecular trio that drives cellular machinery. What’s even more incredible is how these components perform remarkably similar functions in every organism, from bacteria to humans. The genetic code itself is interpreted in a nearly identical way across the living world, and even the ribosomes—those tiny factories that churn out proteins—share a surprising uniformity in their size, structure, and components, no matter the type of cell.

But here’s where things get really intriguing: how should we make sense of this uniformity? Could it point to a shared origin for all life on Earth? Or perhaps some kind of universal design? Either way, the fact that most living organisms are built on the same biochemical foundation suggests that these biological principles arose early in the history of life on Earth. Nobel Prize-winning biochemist Jacques Monod supports this view, stating:

“We have no idea what the structure of a primitive cell might have been. The simplest living system known to us, the bacterial cell… in its overall chemical plan is the same as that of all other living beings. It employs the same genetic code and the same mechanism of translation as do, for example, human cells. Thus, the simplest cells available to us for study have nothing ‘primitive’ about them… no vestiges of truly primitive structures are discernible.”³

In an intriguing way, cells demonstrate a form of ‘stasis’. Bruce Alberts, the President of The National Academy of Sciences of the USA, notes that “we have always underestimated cells.”⁴ He’s right. The entire cell can be viewed as a factory that contains an elaborate network of interlocking assembly lines, each made up of large protein machines. These protein machines, much like human-invented machines, contain highly coordinated moving parts that efficiently carry out tasks. It is hard for us to get any kind of grasp of the seething, dizzyingly complex activity that occurs inside a single living cell.  It’s mind-boggling.

So, what about the first cell? It makes sense to assume it started as something far simpler, like a protocell, which eventually leads to the formation of a “basic” cell capable of self-replication. Nature has the ability to work wonders, and that given the amount of time available, perhaps the impossible is possible. This is where abiogenesis comes in. It’s a theory of chemical evolution that suggests that life began from non-living matter through self-organising natural processes. When you think about the immense spans of time stretching across Earth’s history, the idea starts to feel surprisingly intuitive—an extraordinary transformation unfolding slowly but surely over billions of years.

The Birth of Life: Understanding Abiogenesis

Evolution is split into two tales: first, the chemical, then the biological. While both are part of the same epic, they’re far from the same process. Chemical evolution shouldn’t be confused with its biological successor, as they represent distinct phases in life’s origin story. Biological evolution, driven by processes like natural selection and genetic variation, requires self-replicating entities capable of mutation and adaptation. Chemical evolution, however, is the earlier story of how these first self-replicating molecules arose, setting the stage for everything that followed. What this means is that applying concepts from biological evolution or neo-Darwinism to chemical evolution is generally premature.

Chemical evolution describes how simple, inanimate chemical compounds on early Earth, governed by the basic rules of physics and chemistry and influenced by random factors such as molecular distribution and chemical reactions, gradually combined to form the essential components of life and eventually the simplest self-replicating biological forms.

How is this believed to have played out? Start with Earth’s early atmosphere, a “reducing” environment rich in gases like methane, ammonia, hydrogen, and water vapour, but without free oxygen. This environment, where molecules gain electrons or hydrogen, was ideal for creating organic molecules.

As Earth cooled from its molten beginnings, it reached temperatures that allowed for organic molecules to thrive. Energy sources also abounded: Lightning crackled across the sky, geothermal vents hissed, seismic waves pulsed through the ground, and intense ultraviolet sunlight bathed the surface. These forces acted as catalysts, driving countless chemical reactions in the atmosphere and oceans, birthing a diverse array of organic molecules. High above, ultraviolet light from the sun broke through the atmosphere, creating amino acids and other organic compounds. Closer to the surface, electrical storms and thunder’s shockwaves spurred the creation of similar molecules. Over time, these organic substances gathered, especially near hydrothermal vents or tidal pools, forming a dense, nutrient-rich “prebiotic soup”—a promising broth of life.

Within this primordial soup, simple organic molecules linked up to form longer chains called polymers. The next crucial step was the development of protocells—bubble-like structures with lipid membranes that could maintain their internal chemistry distinct from the outside world. Despite their simplicity, these protocells were resilient enough to withstand Earth’s harsh early conditions.

As protocells evolved, they grew more complex. An essential phase in this narrative was the emergence of self-replicating molecules. Within protocells, certain RNA molecules may have begun to catalyse their own replication, leading to the first rudimentary forms of genetic information transfer.

RNA, or ribonucleic acid, is a crucial biological macromolecule found in all living cells. It plays a key role in converting genetic information, regulating gene expression and catalyses biochemical reactions within cells.

The RNA World Hypothesis (we will get onto this later in the book) suggests that early forms of life relied on RNA both to store genetic information and to catalyse chemical reactions. RNA molecules have the unique ability to act as both genes and enzymes (ribozymes), which could have allowed them to replicate themselves and catalyse other chemical reactions necessary for life. Over time, as these early life forms evolved, the system became more complex and efficient. DNA eventually took over as the more stable medium for storing genetic information, while proteins became the primary molecules for catalysis, energy conversion, and structural functions within cells. This transition would have been gradual, with RNA still playing a central role in processes like protein synthesis (through mRNA, tRNA, and rRNA) and regulation. 

With the establishment of RNA and later DNA as genetic information carriers, and the development of protein synthesis machinery, early protocells evolved into “true” cells capable of replicating their genetic material. This marked the dawn of biological evolution, driving the diversity of life we see today.

What I have outlined here is a short and simplified narrative of chemical evolution—a supposed testament to the power of time, chance, and the fundamental laws of physics and chemistry in creating the wondrous tapestry of life that surrounds us.

The Miller-Urey Experiment: Simulating Early Earth Conditions

For decades, the question of abiogenesis—how life arose from simple inorganic compounds—has captivated scientists. But is it all just a shot in the dark, or do we have real clues about life’s origins?

The good news is that we’re not entirely in the dark. We can test the waters of the primordial soup, so to speak. By recreating the conditions of early Earth in our labs, we can observe first hand whether the basic building blocks of life could have formed spontaneously. Think of it as turning your lab into a time machine, rewinding to a period when Earth was an unexplored chemical playground.

However, turning back the clock a few billion years is no easy feat. We can’t be certain we’re recreating the exact conditions that existed on early Earth, which means our experiments come with a large degree of uncertainty. The more assumptions we make about the ancient world, the less certain we can be about our results.

Despite these challenges, we must persist in our efforts. In 1952, one of the first major attempts to crack the mystery of life’s origins came in the form of the famous Miller-Urey experiment. This study sought to identify a plausible chemical pathway that could transform the gases thought to make up early Earth’s atmosphere into amino acids—those tiny yet mighty molecules that form the building blocks of proteins and, ultimately, all living cells.

The experiment was the brainchild of chemist Stanley Miller, working under the mentorship of Harold Urey. Miller reported the “first laboratory synthesis of organic compounds under primitive Earth conditions.”⁵ His setup involved passing an electrical charge through a flask containing water vapour, methane, ammonia, and hydrogen but no oxygen, simulating the believed conditions of early Earth’s atmosphere and ocean. The electrified spark mimicked lightning storms thought to be prevalent on the ancient Earth. 

The result? Miller generated a variety of organic compounds, including amino acids. It was the first laboratory demonstration that under the right conditions, the raw ingredients of life could emerge from non-living matter.

In a fascinating leap forward from Miller’s iconic work, a 1983 study managed to synthesize all five nucleic acid bases—the molecular bases of DNA and RNA—in the lab. These bases are vital for storing and transmitting the genetic information in living organisms.

Building on Miller’s groundbreaking experiment, subsequent researchers have explored alternative energy sources that could have been present on prebiotic Earth to drive the synthesis of organic compounds. For instance:

• Heat experiments substituted Miller’s spark generator with a furnace to mimic the heat from volcanic activity.
• Ultraviolet experiments replaced the spark with UV light, exposing the primordial gases to short-wavelength UV radiation, akin to the sun’s rays reaching an early Earth with a much thinner atmosphere.
• Shockwave experiments subjected the gases to brief, intense heat followed by rapid cooling, emulating the effects of shockwaves from thunder or meteorite impacts.

Amazingly, each approach churned out amino acids—some more efficiently than others—with variations in the types of organic compounds produced. The message was clear: multiple energy sources could have facilitated the accumulation of essential biological precursor molecules in Earth’s ancient oceans.

Together, the Miller-Urey experiments and these follow-ups provided a compelling picture that the primaeval ocean may have been rich with organic compounds. From this prehistoric “pantry”, nature could sift, accumulate, and concentrate the wealth of ingredients into a prebiotic soup. And from this humble, chemical beginning, nature could begin on its most ambitious project: transforming simple molecules into the first living organisms.

Fast-forwarding to 2009, John Sutherland and his team at the University of Manchester made significant progress in understanding how the basic components of RNA—believed to be one of the first genetic molecules—could have formed spontaneously from simple chemicals under prebiotic conditions. They demonstrated that ribonucleotides, the building blocks of RNA, could be synthesized from relatively simple starting materials, including cyanamide, cyanoacetylene, glycolaldehyde, and glyceraldehyde. Their work provided a plausible chemical pathway for the prebiotic formation of ribonucleotides, marking an important step toward understanding the origin of RNA.

A decade later, in 2019, Thomas Carell and his team took a different approach by simulating conditions of early Earth and successfully producing precursors to the four nucleobases of RNA from basic prebiotic chemicals. Carell’s team demonstrated how these precursors could form under conditions that closely mimicked those of the primordial environment, shedding light on how the molecular components of RNA might have originated.

While Sutherland’s research focused on the direct assembly of RNA’s building blocks, Carell’s work explored the origins of the nucleobases themselves. All these laboratory findings have filled scientists with optimism about the early stages of chemical evolution.

Assessing the Validity of Chemical Evolution Theory

At this point, you’re probably thinking, “So far, so good. This sounds promising!” And you’re right—it does. But the real test of any scientific theory is how well it holds up under scrutiny. Playing devil’s advocate is a crucial part of the scientific process. It’s how we safeguard against rushing to conclusions or overlooking potential errors. Ignoring this kind of critical examination—especially when it comes to the theory of chemical evolution—would undermine everything that makes science reliable.

So, in that spirit, let’s put the famous Miller-Urey experiments under the microscope and examine the broader implications of their findings.

Challenging the Myth of the Prebiotic Soup

For years, scientists believed that the early Earth was largely hospitable to chemical formation—an environment where the ingredients for life could have swirled in a rich “prebiotic soup,” potentially sparking the origin of life. But recent discoveries have thrown a wrench into this comforting idea. New research paints a much rougher picture of our planet’s primordial environment—one that was far less welcoming to the first stirrings of life than we’d like to imagine. This shift in perspective is forcing scientists to return to the drawing board and reconsider some long-held assumptions about the conditions that gave rise to life.

One major hurdle lies in the inherent dilution processes prevalent in the atmosphere and the ocean.  Chemical evolution relies on polymerization, where simpler molecules (monomers), like amino acids, connect to form long organic chains called polymers. However, in a water-rich environment like the prebiotic ocean or a hypothetical prebiotic soup, the odds of polymerisation occurring are particularly low. According to researchers like Jeffrey Bada and Steven Cleaves, who studied “the origin of biologically coded amino acids”, both Earth’s oceans and atmosphere would have scattered life’s building blocks too thinly for significant chemical reactions to take place.⁶ Astrobiologist Paul Davies echoes the concern, suggesting that if a “prebiotic soup” ever existed on Earth, it was likely so weak and watered-down that the chances of crucial chemical reactions taking place were slim to none.⁷ The dilute nature of such an environment would make the spontaneous formation of these critical chains of molecules an uphill task. Imagine trying to build a sandcastle at the beach while waves keep washing away your progress—that’s what polymerisation faces in water. As the U.S. National Academy of Sciences explains, “Two amino acids do not spontaneously join in water. Rather, the opposite reaction is thermodynamically favoured.” In other words, water doesn’t play nice—hydrolysis (the breakdown of polymers into monomers) is thermodynamically favoured over condensation (the formation of polymers from monomers).

Faced with this dilution dilemma, scientists have started exploring ways nature might have fought back. The idea? Some special spots on early Earth could have acted like concentration zones, gathering life’s essential molecules and giving them a better shot at reacting with one another. These include evaporating pools in coastal regions, microscopic water channels within ice formations, adsorption onto mineral surfaces, thermal gradients in porous rocks, and hydrothermal vent systems. While these environments could theoretically provide conditions for concentrating organic molecules, experimental evidence supporting their effectiveness remains limited, and each proposed mechanism must account not only for the concentration of molecules but also for maintaining conditions suitable for the complex chemistry required for life’s emergence.

Take tidal pools, for instance. As water evaporates, molecules can get packed into tighter spaces, improving their chances of combining in new ways. But tidal pools also face wild shifts in pH and temperature, which can destabilise molecules and increase the risk of hydrolysis. In ice environments, while liquid water veins between ice crystals can concentrate molecules through freezing-induced exclusion, the low temperatures significantly reduce molecular collision rates and reaction speeds. Then there are mineral surfaces, such as clays and metal oxides, which can gather organic molecules by attracting them through adsorption and electrostatic forces. But here, the problem is that the molecules tend to bind too tightly—a process called over-adsorption—which can restrict their movement and prevent them from forming the longer chains needed for prebiotic chemistry.

And then there’s the energy problem. Energy is a bit of a double-edged sword when it comes to life’s beginnings. On the one hand, energy is absolutely necessary to organise molecules into complex structures. On the other hand, too much raw energy can be downright destructive. It’s like giving a toddler superhuman strength. Sure, they might accidentally create something amazing, but let’s be real—they’re far more likely to smash everything to bits.

The energy sources available on early Earth—things like UV radiation from the Sun, volcanic heat, or lightning strikes—weren’t exactly gentle tools. Sure, they might occasionally help stick some molecules together, but they were just as likely to destroy them. Modern research backs this up. For example, Bada and colleagues have shown that ultraviolet light, while capable of catalysing certain chemical reactions, often breaks down the very molecules it helped create.⁸ Geothermal and volcanic activity, while potential sources of chemical energy, often prove too harsh for organic compounds. The high temperatures around volcanoes and some hydrothermal vents typically break down organic molecules. Research by Johnson and Li (2018) in the Journal of Prebiotic Chemistry found that vents can indeed help synthesise important biomolecules like amino acids.⁹ But there’s a catch—those same vents often get so hot and unstable that they destroy the molecules before they can participate in further reactions. 

Similarly, the role of electrical discharges, such as lightning, also presents a dual-edged sword. The classic Miller-Urey experiment demonstrated the potential of electrical discharges to synthesise amino acids and other organic molecules from simple gases. However, a landmark study by Anderson et al. (2020) in “Origins of Life and Evolution of the Biosphere” revisits the classic Miller-Urey experiments with a focus on the degradation pathways of complex organic molecules under simulated lightning conditions.¹⁰ Their findings suggest that while electrical discharges can help form essential biomolecules, they also carry a high risk of breaking these molecules down again.

So, the interplay between various energy sources on early Earth presents a complex scenario in the context of chemical evolution. These energy sources had a double-edged nature: they could fuel the synthesis of essential organic molecules, but at the same time, they risked tearing those fragile molecules apart.

In reality, the experimental setups employed to investigate life’s origin often fall short of authentically replicating the chaotic, uncontrolled conditions of early Earth. Typically, these experiments typically isolate and regulate each energy source—out of necessity. However, this controlled approach doesn’t reflect the ever-changing environment of early Earth, where multiple forces like lightning, UV radiation, and volcanic activity acted simultaneously and unpredictably. As Dr. Ian Fry aptly puts it, the disconnect between controlled laboratory conditions and the reality of these multifaceted and interdependent energy conditions can result in a significant gap in our understanding of life’s origins.¹¹

To address this, scientists often use “traps”—a clever lab technique that protects newly formed organic molecules from destruction by the very energy sources that created them. While this selective control helps scientists preserve reactions in the lab, it doesn’t reflect what would have happened naturally. Nature does not discriminate; it offers no inherent protective measures to shield emerging organic molecules from the destructive impacts of environmental energies. The laboratory experiments, with their carefully controlled settings, don’t replicate the chaotic and unpredictable conditions of early Earth, and this gap is important to keep in mind when we try to draw conclusions about what these experiments might tell us.

To summarise, the hypothesis of a ‘prebiotic soup’ as the cradle for the emergence of life on Earth encounters several challenges that cast doubt on its plausibility:

• Destructive Interactions: The various forms of energy on early Earth would likely have resulted in damaging interactions that could have significantly diminished, if not entirely consumed, essential precursor chemicals. This constant cycle of creation and destruction could have significantly slowed down, or even halted, chemical evolution.
• Dilution Problems: The envisioned ‘prebiotic soup,’ whether imagined as spanning vast oceans or contained within smaller pools, was likely too dilute to support direct polymerisation. This dilution issue challenges the feasibility of achieving the necessary concentrations of organic molecules for life’s precursors to form and evolve.
• Lack of Geological Evidence: There is a conspicuous absence of concrete geological evidence supporting the existence of an ‘organic soup’ on the primitive Earth. Despite extensive research, no direct proof has been unearthed to affirm the presence of this crucial primordial broth.
• Experimental Limitations: Laboratory experiments designed to recreate the conditions of early Earth and explore the origins of life frequently fall short of capturing the complex, dynamic, and often chaotic nature of our planet’s nascent ecosystems. These models fail to simulate the delicate balance between the constructive roles of energy sources in synthesising organic molecules and their destructive potential. Furthermore, the use of traps and other methodologies in these experiments, intended to protect synthesised organic products from degradation, does not reflect the unselective and unshielded conditions of the natural world. 

Early Earth’s Atmosphere: Not So Welcoming After All

Here’s the thing about oxygen: while it’s essential for life as we know it today, it would’ve been a real buzzkill for the formation of life’s building blocks billions of years ago. Even tiny amounts of oxygen in the atmosphere could have put a stop to the creation of the organic molecules needed to kickstart life. Why? Because oxygen creates oxidising conditions that make it nearly impossible for these crucial compounds to form—and if they somehow did, they’d quickly break down. That’s why scientists, when recreating the conditions of early Earth in the lab, purposely leave oxygen out of the mix. Without it, molecules like amino acids have a fighting chance to form and stick around.

But here’s the twist: Earth’s atmosphere wasn’t as simple as the “zero-oxygen” scenario long believed. Recent research has revealed that small amounts of free-oxygen were likely floating around much earlier than scientists had thought, complicating our understanding of how life arose. 

This is supported by findings of oxidising minerals and calculations hinting at the production of oxygen through the breakdown of water-based chemical compounds.¹² A study published in the journal Science in 2007 found that certain iron formations from 2.5 billion years ago could only have formed if there was some free oxygen in the atmosphere.¹³ In a further study published in the journal Nature in 2014, researchers provided evidence of early oxygenation of the Earth’s atmosphere.¹⁴ This study, based on the analysis of ancient Australian rocks, suggested the presence of small amounts of oxygen about 3 billion years ago. Even more astonishingly, isotopic studies of sulphur published in Geochimica et Cosmochimica Acta, points to the presence of oxygen around 3.8 billion years ago.¹⁵

This paints a far more complex picture of Earth’s atmosphere during its formative years. If oxidising conditions were around that early, the traditional idea of an entirely oxygen-free environment—primed for life’s building blocks—is oversimplified. The presence of oxygen would have made early Earth less conducive—or even detrimental—to the emergence of life. It’s no longer as simple as “no oxygen, no problem.”

Moreover, the Miller-Urey experiments originally assumed that Earth’s early atmosphere was primarily made up of methane, ammonia, and hydrogen. Back in the 1950s, scientists believed this cocktail closely mirrored Earth’s early atmosphere: reducing gases with no oxygen in sight. But by the 1980s, it became clear that the early atmosphere was less stable than the methane-rich, oxygen-free atmosphere once believed. A major shift in the scientific consensus followed, with experts realising that early Earth’s atmosphere looked quite different. In fact, as a 1980 Science journal article bluntly stated:

“No geological or geochemical evidence collected in the last thirty years favours an energy-rich, strongly reducing primitive atmosphere (i.e., hydrogen, ammonia, methane, with no oxygen). Only the success of the Miller laboratory experiments recommends it.”¹⁶

Fast forward to the 1990s, and the gap between the classic Miller-Urey experiment and our evolving understanding of early Earth grew wider. By 1995, Science declared that the portrait of the early atmosphere painted by the Miller-Urey experiment bore little resemblance to reality.¹⁷ This sentiment was reinforced in 2008, when the journal reported, “Geoscientists today doubt that the primitive atmosphere had the highly reducing composition Miller used.”¹⁸ This body of evidence suggests that the assumed atmospheric conditions of the Miller-Urey experiments likely require a significant overhaul. Unfortunately, this revision doesn’t favor the original hypothesis. Instead, it implies that chemical evolution was probably less plausible than the Miller-Urey experiments initially suggested.

The Indispensable Role of Human Intervention

Earlier, we briefly touched on experimental limitations, but let’s dive deeper. The Miller-Urey experiment and subsequent studies aimed to recreate the conditions for life’s spontaneous emergence on Earth. However, there’s a catch: these experiments, while revolutionary, weren’t exactly “spontaneous.” They were meticulously designed and tightly controlled by scientists—a far cry from the chaotic, unpredictable environment of ancient Earth. This discrepancy significantly impacts how we interpret their implications for life’s origin.

Consider ultraviolet (UV) light, for instance. In origin-of-life research, scientists use UV light to simulate the sun’s radiation and its potential effects on chemical evolution. However, they often cherry-pick specific types of UV light—usually shorter wavelengths—because longer ones can be destructive to organic compounds. This selective approach differs markedly from the indiscriminate nature of solar radiation on early Earth, which would have exposed prebiotic materials to the full spectrum of UV light, both beneficial and harmful.

Then there’s the issue of using other energy sources like heat, electrical sparks (to simulate lightning), and shock waves. For instance, replicating the extreme heat from volcanoes or steam vents is tricky. While these natural heat sources might well have played a role in early life, they were likely spread out and short-lived, making it hard to imagine them consistently driving continuous synthesis. Simulating lightning effects through electrical discharges is another challenge. Real lightning generates extremely high temperatures that could easily destroy nascent organic compounds rather than facilitate their formation.

At every turn, these experiments face a problem: the controlled environment of a lab, necessary to produce organic compounds, does not mimic the messy, unpredictable conditions of early Earth. The prebiotic world wasn’t just a static “test tube” but a dynamic soup of countless reactions and forces. Why assume chemical reactions will behave the same way isolated in a lab as they would in the dynamic, complex environment of early Earth? Scientists refer to this interplay as the “Concerto Effect,” where chemical reactions don’t exist in isolation but mix, amplify, and interfere with one another in unexpected ways. In our probiotic world, this likely led to destructive outcomes that hinder or completely halt the synthesis of more complex compounds.

Here’s where the tension lies: To make these experiments work, scientists must carefully adjust the conditions—tweaking variables like atmospheric composition, energy inputs, and reaction isolation—to coax reactions toward a desired outcome. In doing so, they unintentionally introduce an element of design into a system meant to represent prebiotic Earth. This intelligent “nudge,” while necessary to get results, raises some big philosophical questions. Think about it this way: Whenever researchers direct a reaction sequence or impose particular constraints upon a chemical system that are foreign to the system they are attempting to model, aren’t they effectively introducing an element of information (foresight) into that system? This act of introducing information is not merely a manipulation of chemical states; it is an implicit acknowledgement of an overarching intellectual order. 

This isn’t to say origin-of-life experiments are invalid or unimportant—they’ve taught us a ton about possible chemical pathways that could have contributed to life. But they also highlight just how much we rely on intelligent input to make biologically relevant chemistry happen. Without some form of intelligence acting on the process, life does not appear to spontaneously emerge from random molecular interactions.

The Challenge of the Spontaneous Assembly of Life’s Essential Chemicals

For argument’s sake, let’s assume that the early Earth was conducive to organic molecules, with a prebiotic soup teeming with life’s elementary building blocks (though both are far from certain). Even then, we face the huge challenge of figuring out how these raw materials somehow evolved and organised themselves into the very first spark of biological life.

Here’s the tricky part: in the absence of a living biological agent, molecules don’t exactly have ambitions. They don’t naturally decide to band together and “evolve” toward becoming alive. Molecules are indifferent to the whole concept of life. Sure, once life exists, living organisms can cleverly exploit chemical reactions to grow, survive, and reproduce. But today, we don’t observe molecules spontaneously assembling into anything that bears even the slightest resemblance to a living cell without the influence of pre-existing life.

This issue is something that James Tour, a leading Professor of Chemistry, Materials Science, Nanoengineering, and Computer Science at Rice University, has spent a lot of time talking about. Recognised as one of “The World’s Most Influential Scientific Minds” by Thomson Reuters, Tour has highlighted some major gaps in our understanding of how life began from a spontaneous point of view. And honestly? Those gaps are so big, they make the Grand Canyon look like a pothole. Let’s dig in:

(1) Chirality: One of the most curious quirks of biology is something called chirality, or molecular handedness. Think of your hands—they’re mirror images of each other. You’ve got a left hand and a right hand, but no matter how hard you try, you can’t make your left hand fit perfectly into your right glove. The same idea applies to many of the molecules that make up life—like sugars, amino acids and fats. They exist in two “flavours,” left-handed and right-handed. The really weird part? Life on Earth has a strict preference: amino acids (the building blocks of proteins) need to be left-handed, and sugars need to be right-handed. 

It might sound like a small detail, but this consistency is absolutely critical. Molecules in living systems rely on their shape and handedness to interact properly. If you switched a left-handed amino acid for a right-handed one, it could completely mess up a protein’s ability to fold into the precise shape it needs to perform its job. Life exclusively uses L-amino acids and D-sugars. But here’s the real head-scratcher: if we rewind the clock back to early Earth, when life was just starting to emerge, things wouldn’t have been so organised. Since ordinary chemical reactions lack inherent bias, then in the “primordial soup” where life supposedly began—you’d expect to find an equal mix of left- and right-handed versions of these molecules. But then the odds of randomly making a protein out of only left-handed amino acids in such a scenario are incredibly low. For instance, a protein with 100 amino acids has a 1-in-2¹⁰⁰ chance of being purely L-form in a racemic environment. If just one right-handed D-amino acid is incorporated into a protein chain, it can disrupt the protein’s proper folding and function. Proteins need to fold into very specific shapes to work properly, and a single wrong-handed amino acid can throw everything off, rendering the protein unable to perform its intended biological role. Since proteins do most of the heavy lifting in cells (like speeding up reactions or building structures), this precision is absolutely critical.

So here’s the question: how did life on early Earth manage to only use left-handed amino acids and right-handed sugars? Without any lab techs or fancy equipment tampering with the mix, what tipped the scales? How did the early biochemical processes select for L-amino acids over their D counterparts?

There are a few intriguing ideas. These include the possibility of chiral selection through polarised light, asymmetric synthesis catalysed by minerals, or a statistical fluctuation in the early prebiotic environment that was amplified over time. Fascinating as these ideas are, it’s incredibly hard to replicate these processes in a lab. Even with today’s cutting-edge technology, scientists struggle to recreate the kind of flawless handedness that life achieves naturally.

And the challenge doesn’t end there. These molecules don’t just have to be the right handedness—they also need to connect in very specific ways, a concept known as regiochemistry, and their atoms need to be arranged just so (stereochemistry). These factors are crucial for how molecules behave and interact with each other.

Even with all our tools, knowledge, and technology, creating the molecular uniformity and precision found in life is a humongous task in modern science. If we can barely replicate the intricate and precise molecular configurations seen in the natural world, how on earth did a primordial soup, without any conscious directing force, figure it out billions of years ago? There is an intuitive answer here: It probably didn’t.

(2) Selection mechanisms: When you think about building something as complex as a “simple” cell, even a protocell, every chemical element has to be lined up in just the right order. But with no clear instructions, no guiding hand, and no prewritten plan, how does a chaotic, soupy mess, achieve such a feat? Are chemical gradients, electrostatic forces and self-organising processes enough? In the supposed primordial mix of random molecules floating about, there were no obvious “conductors” or “selectors” to organise the process. It’s hard to imagine how, in such a random environment, the right molecules could have come together in the exact sequence needed for life. Absent of a directing force, this primordial mixture seems to lack any system for determining which molecules to select and at which stage they should be integrated to progress towards life.

Entertaining the idea for a moment, supposing there were some kind of selectors in that ancient environment, responsible for picking out the right molecules. These selectors would have to be pretty sophisticated—maybe even more complex than the molecules they were choosing. But this raises another tricky question: how did these selectors come about? Who or what “selected” them? It’s like an endless loop—selectors would need other selectors to choose them, and so on. So, we’re left wondering: how could such a complicated selection process emerge from what seems like a completely unorganised environment?

Why does this matter? Because the process of building life isn’t forgiving. Unlike tinkering with LEGO bricks, where a wrong piece can easily be swapped out, molecular chemistry doesn’t work that way. An incorrect chemical insertion can halt the entire process. Once a molecule is integrated, its removal or correction is not straightforward. In the complex world of molecular synthesis, it’s often impossible to isolate and remove a distinct part of a molecule once it has been incorporated. Like a sculptor chiselling a statue: one wrong strike and the entire piece could be ruined.

And there’s another problem: there’s no memory in this process. There’s nothing keeping track of mistakes or preventing them from happening again. If an error occurs, there’s no guarantee that things will reset and try again—it might just be game over. And even if the process does start over, there’s nothing stopping it from making the exact same mistake.

(3) Purification: For abiogenesis to occur, you need a system that can separate the good stuff from the junk. If contaminants aren’t removed, they’ll hog resources and prevent the essential molecules from doing their job. But how could a probiotic system, with no obvious ability to “choose” between useful molecules and waste, pull this off? Even if we assume that some basic organic polymers could form naturally, that’s just the start. Life requires more than raw materials—it needs a safe space where important chemical reactions can happen.

Many scientists believe that one of life’s first breakthroughs might have been the creation of a membrane. Imagine an early protective bubble—a barrier that could separate the inside from the outside world while still letting nutrients in and waste out. Without such a shield, early molecular systems would have been bombarded by harmful chemicals, unable to gather what they needed to grow, metabolise or evolve.

But here’s where things get interesting. In modern cells, the membrane is much more than a passive barrier. Known as the “lipid bilayer,” it acts like a highly intelligent gatekeeper. This structure doesn’t just protect the cell; it actively controls what flows in and out. Water, nutrients, and essential ions are welcomed inside, while waste products are swiftly expelled. Embedded in the membrane are incredible protein machines that discriminate between beneficial and harmful substances, using sophisticated molecular pumps and pathways to keep everything just right.

Scientists have made some progress in understanding how early versions of these membranes might have worked. Experiments with simple vesicles made from lipids show that these structures can form naturally and allow certain molecules to pass through selectively. Synthetic biology has even created artificial membranes that mimic some of these properties, giving us clues about how early life might have managed to transport essential nutrients while keeping harmful substances out. But none of these studies show that this process could happen spontaneously in nature; if anything, it’s the opposite. Modern membranes are incredibly complex, boasting passive transport channels, active pumps, and intricate molecular machinery—all of which were absent in the primordial world. No origin-of-life experiment has successfully replicated the full suite of necessary functions that cell membranes achieve so effortlessly. Modern cells solve purification with exquisitely engineered membranes and pumps—protein machines that act like bouncers, sorting nutrients from waste. But for life to emerge without such machinery, nature needed a way to filter, organise and protect its first fragile biomolecules.

Proposed pre-biotic solutions sound plausible at first. Mineral surfaces, like iron-sulfide bubbles near hydrothermal vents, might have corralled early reactants. Simple fatty membranes could have formed protective bubbles. Environmental cycles, like repeated drying and rewetting, may have concentrated key molecules. Yet these processes lack the precision biology demands. For instance, while minerals can trap some organic molecules, they’re equally hospitable to destructive contaminants. Primitive membrane bubbles, while good at encapsulation, would have leaked constantly, diluting any advantage. Experiments show that without active transport systems—which require genes to encode them—vesicles quickly fill with molecular debris, turning potential “life cradles” into toxic dumpsters.

Even more challenging is the coordination required. Imagine a scenario where mineral filters, membrane bubbles, and replication processes all align perfectly in time and space—a hydrothermal vent that simultaneously sorts molecules, encapsulates them, and jumpstarts replication before degradation kicks in. Such a Goldilocks scenario hinges on countless variables: pH levels that suit both RNA stability and mineral chemistry, temperatures that permit lipid assembly without destroying fragile organics, and cycles timed to molecular lifetimes. While lab experiments can mimic individual steps with careful tweaking, no natural environment has been shown to orchestrate this symphony of events autonomously.

The core paradox remains: life’s purification systems depend on genetic instructions, but those instructions couldn’t have survived without purification. It’s a biological Catch-22. How such a complex system could have emerged spontaneously stretches the bounds of plausibility.

(4) Chemistry is fragile: The creation of life’s basic building blocks involves a complex series of chemical reactions that are highly sensitive to their environment. Factors like temperature, pressure, the type of solvent, light exposure, pH levels, and the gases in the atmosphere all need to be fine-tuned to encourage the formation of complex molecules. Otherwise, the chemistry could easily veer off course, leading to countless dead ends. Take peptides, for instance—these chains of amino acids are essential for proteins. To form peptides, amino acids must undergo a condensation reaction, where water is removed. This step often requires specific catalysts or energy sources to proceed efficiently.

Many organic molecules are inherently unstable. They can easily degrade when exposed to conditions like UV radiation or water, making it difficult to preserve these fragile compounds long enough for them to participate in subsequent reactions or self-assemble into larger structures. Furthermore, isolating specific reactions is crucial to prevent unwanted interactions between different molecules.

In the lab, scientists must carefully orchestrate these processes. This involves a deep understanding of how molecules behave under various conditions and how catalysts or inhibitors can steer reactions in the desired direction. Every step demands meticulous monitoring and analysis because even minor missteps can cause the entire process to fail.

Despite decades of research, the sheer number of chemical steps required to create even the simplest molecules found in a basic cell remains only partially understood. The assembly of larger, more complex structures necessary for a functioning cell is even more daunting. Therefore, the notion that life’s precursor molecules could have spontaneously emerged and assembled into complex structures near environmental features like volcanoes stretches credulity. The natural assembly of materials through such a complex, multistep synthesis without explicit design or intention remains counterintuitive.

(5) Specificity: One of the most critical hurdles in biology is the remarkable sequence specificity required for proteins to function. It’s not enough to just string together amino acids like beads on a necklace—most random sequences won’t cut it. Instead of forming useful proteins, they usually end up as non-functional chains or, even worse, misfold into shapes that clump together and form harmful aggregates. This precision is crucial because a protein’s function depends on its amino acid sequence and its ability to fold into a unique three-dimensional shape.

Just how complex is this? Researchers like Peter Tompa from the University of Brussels and George Rose from Johns Hopkins University suggest that the potential number of protein-protein interactions in a single cell could be as high as 10^{79,000,000,000}.¹⁹ Each functional protein has to be assembled from a highly specific sequence of amino acids, and then it must fold correctly into its final shape. Any error in this process—whether in the sequence or the folding—can result in a useless protein, or worse, one that causes damage by forming toxic aggregates.

But the complexity doesn’t stop with proteins. RNA, another superstar molecule of life, faces similar challenges. For RNA to work properly, it needs to be built from the right sequence of nucleotides and fold into precise three-dimensional shapes—just like proteins. RNA synthesis and folding are influenced by various factors, including the chemical environment and catalysts. The idea that RNA, DNA, or proteins could spontaneously emerge from simple chemical reactions driven by vague “dynamic forces” oversimplifies the processes of assembly, polymerisation, and sequencing required for even the most basic forms of life.

This complexity has led researchers to explore various hypotheses about the origin of life. One of the more popular ideas is the “RNA world” hypothesis, which suggests that RNA molecules capable of catalysis and self-replication might have been the precursors to life as we know it. However, as we will discuss later, this hypothesis faces significant challenges that make it unlikely to fully explain the origin of life.

What becomes clear is that the journey from simple chemicals to the first living organisms was far from straightforward. Every stage—from the assembly of amino acids and nucleotides to the folding of proteins and RNA—required precise conditions and mechanisms. Each step introduces new challenges that had to be overcome, making the road to life an extraordinarily complex and finely balanced process.

(6) The Role of Time in Life’s Origins: Friend or Foe? When it comes to unravelling the mystery of life’s origins, time is often seen as a key player. The prevailing assumption is that, given enough time—spanning hundreds of millions or even billions of years—the essential molecules for life would naturally form, assemble, and evolve into the earliest living systems. But what if time isn’t always the helpful ally we imagine? What if it’s more of a double-edged sword? In the context of chemical synthesis, particularly concerning the formation of kinetic products pivotal for generating life’s organic molecules, time can paradoxically serve as a hindrance. 

Nobel Laureate, Richard Roberts, has pointed out that synthetic reactions lack an inherent mechanism to cease. In a prebiotic world, without specific intervention, these reactions continue until the reactants are depleted or until external conditions intervene to stop the process. There’s no prebiotic off-switch to halt a chemical process once it has produced the right molecules necessary for life. Instead, they continue, consuming reactants and producing an array of unwanted by-products and derivatives.

In a prebiotic environment, this lack of control could be disastrous. Without the ability to stop at just the right moment, these chemical reactions are likely to go too far. The longer the reactions run, the more likely they are to veer off course, making it harder to isolate the specific compounds that are key to forming life as we know it.

This paints a paradoxical picture. While we often think of time as providing ample opportunity for life’s precursors to emerge and evolve, too much time can complicate matters. Instead of encouraging the formation of life, unchecked reactions over vast periods could make the process even more difficult.

Given the extraordinary complexity required in molecular sequencing, the exact conditions necessary for chemical reactions, and the intricate array of functional structures that must align perfectly in the processes leading to the origin of life, it becomes increasingly difficult to support the idea that life emerged spontaneously. The leap from non-living matter to living organisms demands a staggering level of order and precision—something that purely unguided natural processes seem unlikely to accomplish on their own. Even with our most advanced technology and intelligent intervention, we have yet to successfully replicate the intricate steps required for biological life, which raises serious doubts about the likelihood of a purely naturalistic explanation for life’s origins.

Entropy, Information, and the Unresolved Challenge of Life’s Origins

The origin of life hinged on a cosmic tug-of-war between order and disorder, a story rooted in the principles of thermodynamics. Specifically, how did life’s incredible complexity emerge in a world seemingly destined for disorder? How do complex biological macromolecules, like DNA and proteins, form spontaneously in an environment subject to entropy?

Entropy is a concept in physics that, at its core, measures how disordered a system is. Entropy is the universe’s way of reminding us that nothing lasts forever. It’s a term from physics that describes how everything, from a carefully built sandcastle to a star in the cosmos, tends to move from order to disorder. This idea comes from the second law of thermodynamics, which tells us that the total entropy—or disorder—of the universe always increases over time. In other words, the universe “prefers” messiness. Think about it: creating something orderly, like a vase, takes time and energy, but breaking it happens in a split second. Entropy works the same way on a cosmic scale. Energy spreads out, systems become less efficient, and even the most stable structures eventually breakdown.

Scientists like Sadi Carnot, Rudolf Clausius, and Ludwig Boltzmann helped define and explain entropy over the last two centuries. Carnot first noticed that no machine could be perfectly efficient—some energy is always lost as useless heat. Clausius later introduced the term “entropy” in 1865, from the Greek word for “transformation,” while Boltzmann connected entropy to probabilities, showing there are far more ways for particles to arrange themselves in a disordered state than in an orderly one.

At its heart, entropy explains why chaos is the natural tendency of the universe. It’s why things fall apart, why life feels so delicate, and why perfection seems so fleeting. 

How does this universal drift toward disorder relate to the origin of life? The question is simple: How could life’s essential macromolecules, which are highly ordered structures, arise from simpler, more disordered precursors like amino acids, sugars, and phosphates, in a universe that trends towards increasing entropy (disorder)?

The answer lies in a surprising twist: while the second law of thermodynamics says that the total entropy (disorder) of the universe must always increase, local pockets of order can form, as long as the overall entropy still climbs. This idea is captured by the term “negative entropy,” or “negentropy.” Though it may seem counterintuitive, systems can become more ordered when they are part of a larger, open system that exchanges energy and matter with the environment.

Think about ironing a wrinkled shirt. You’re imposing order by smoothing out the fabric, which reduces its entropy. But this doesn’t break any natural laws because the energy you use—both from your body and the hot iron—releases heat and increases disorder elsewhere, like in the environment. So, while the shirt becomes more orderly, the total entropy of the entire system (you, the iron, and the room) still goes up.

This same principle might help explain how life’s first molecules formed. Early Earth was an “open system,” meaning it constantly received energy inputs from external sources like sunlight, lightning, and geothermal heat. These energy flows could drive localised decreases in entropy, allowing simpler molecules like amino acids and sugars to assemble into more complex macromolecules, such as proteins or RNA. Essentially, raw energy acted like a cosmic ironing board, temporarily countering the natural pull toward disorder and enabling the building blocks of life to come together.

Of course, there are still challenges. Earth’s ability to foster local order is always temporary—it depends on a constant influx of energy. This raises doubts about whether it could sustain the conditions needed for life over time. Regardless, the popular census is that steady energy flow meant that environments like hydrothermal vents or sunlit pools could maintain just the right conditions for fostering chemical complexity.

But this is where we get carried away—while it’s true that energy can create order, it doesn’t automatically mean that molecules will organise themselves into something as complex as life. To understand why, we need to make an important distinction: order and the complexity of life are not the same thing.

Take a moment to think about DNA. It’s not just the molecule’s structure that matters—what makes DNA extraordinary is the information it carries. As the famous duo Francis Crick and James Watson revealed, biology is fundamentally about instructions encoded in molecules. Information is what separates life’s dazzling complexity from mere chemical organisation.

Let’s break it down with an example. Think about a salt crystal. At first glance, it seems impressive—sodium and chloride ions arranged in a perfectly ordered, repeating pattern. No matter where you look, it’s the same predictable structure: sodium, chloride, sodium, chloride. This kind of arrangement is wonderfully orderly, no doubt, but it doesn’t carry much information. Once you understand the basic rule—sodium alternates with chloride — you’ve cracked the code. There are no surprises, no deeper meaning. It’s all repetition. Orderly? Yes. Full of information? Not so much.

Now imagine a heap of random polymers, and in this case, they’re all mixed up with no particular order or pattern. Sure, the polymers themselves are complex molecules, but because they’re arranged randomly, there’s no real functional organisation. So, while the system is complex, it’s completely chaotic and lacks any meaningful information.

Biological life, on the other hand, is something else entirely. It hits the sweet spot where order and complexity come together in a way that creates information. Scientists often call this “specified complexity.” A great example is DNA. The sequence of bases in DNA (adenine, thymine, guanine, and cytosine) isn’t just random, nor is it repetitive like the salt crystal. Instead, these bases are arranged in a specific order to encode instructions for making proteins. It’s like a biological blueprint—highly ordered, but also filled with information. 

This is what sets life apart from mere chemistry. A salt crystal might be beautifully ordered, but it doesn’t do anything beyond just sitting there. A chaotic jumble of polymers might be complex, but it doesn’t hold the instructions for anything useful. DNA—and life in general—combines the best of both worlds. It’s ordered enough to be functional and structured, but complex enough to carry detailed information. But here’s the real puzzle: can energy, coupled with natural processes to focus and filter,  create information? Order? Yes, maybe. Repetition? Possibly. But information—that’s a different beast altogether. Edward Steele and his thirty-two co-authors, across eleven countries, in ‘Progress in Biophysics and Molecular Biology,’ tackled this very question, and concluded:

“The transformation of an ensemble of appropriately chosen biological monomers (e.g., amino acids, nucleotides) into a primitive living cell capable of further evolution appears to require overcoming an information hurdle of super astronomical proportions, an event that could not have happened within the time frame of the Earth except, we believe, as a miracle. All laboratory experiments attempting to simulate such an event have so far led to dismal failure.”²⁰

While thermodynamics does allow the emergence of order from chaos under the right conditions, it also sets a limit on the extent of ‘coding work’ that can occur naturally. In other words, you might get some structure, but you won’t get the kind of complex, organised information that life needs. While negative entropy might explain how some order forms, it isn’t the same thing as creating information. Just as a gold bar cannot emerge from a lump of coal regardless of the energy or effort applied, information cannot be derived from mere negative thermal entropy. Bricks might be necessary to build a house, but a house won’t self-assemble without a blueprint or plan. Similarly, regardless of negative entropy, amino acids or nucleotides won’t spontaneously form functional proteins or RNA without an existing template or set of instructions.

Here’s where the limit of natural processes becomes apparent. The assumption that an open system—a system exchanging energy and matter with its surroundings—can explain life’s complexity is tempting, but it falls short. Amino acids floating around in a warm pond or near a hydrothermal vent aren’t going to self-organise into a primitive living cell just because energy is flowing into the system. Something more is needed—something that nature, on its own, seems ill-equipped to provide. In part two of the book, we will look at this in more detail.

The Hurdle of Self-Replication in Life’s Origin

Self-replication remains one of the most tantalising and perplexing puzzles in science. It’s the ultimate leap from chemistry to an evolving world of biology. Without self-replication, life as we know it couldn’t exist, yet there is so much about this process we poorly understand.

Abiogenesis suggests life began with a series of unguided chemical reactions, culminating against staggering odds in the formation of a simple, self-replicating molecule. This molecule would have been the trailblazer, igniting the evolutionary engine that drives life forward. Natural selection, random mutations, and environmental pressures would have done the rest, slowly transforming that primordial replicator into the first cellular organisms.

But here’s the rub: self-replication isn’t simple. Far from it. It’s a marvel of precision and coordination, more akin to an advanced engineering system than a random chemical fluke. James F. Kasting, a scientist renowned for his work in planetary habitability, pointed out the difficulties in his book How to Find a Habitable Planet. He mentioned that “the origin of a self-replicating molecule, which is capable of undergoing Darwinian evolution, is currently one of the most fundamental problems in science and one that is largely unsolved.” Biologist Eugene Koonin echoed this in his 2007 paper, highlighting that current theories offer intriguing leads but fail to explain how the first efficient RNA replicase or translation system could have emerged:

“Despite considerable experimental and theoretical effort, no compelling scenarios currently exist for the origin of replication and translation, the key processes that together comprise the core of biological systems and the apparent pre-requisite of biological evolution. The RNA World concept might offer the best chance for the resolution of this conundrum but so far cannot adequately account for the emergence of an efficient RNA replicase or the translation system.”²¹

When a cell replicates, it doesn’t just split in half. It undergoes a highly coordinated in-house engineering process. The cell expands, constructs a replica within its own membrane, and then partitions itself, releasing a new cell into its surroundings. This process not only guarantees accurate replication but also shields the cell from disruptive environmental interferences and prevents its components from dispersing into the watery environment. To help you imagine, visualise this process as a car expanding its frame to accommodate a second car, assembling the new components within this protected space, and then constructing a dividing wall to release a fully functional, identical car on the road beside it. While it may sound like something out of the science fiction film series Transformers, this captures the essence of self-replication. A true self-replicating system must autonomously find, acquire, and process materials, generate energy and have feedback and quality control mechanisms.

How could something so intricate arise spontaneously? Even DNA and RNA can’t self-replicate without help. They rely on each other and an array of cellular machinery. Geneticist Michael Denton explains such a feat:

“What we would be witnessing would be an object resembling an immense automated factory, a factory larger than a city and carrying out almost as many unique functions as all the manufacturing activities of man on earth. However, it would be a factory which would have one capacity not equalled in any one of our most advanced machines, for it would be capable of replicating its entire structure within a matter of a few hours. To witness such an act… would be an awe-inspiring spectacle.”²²

Richard Dawkins claimed in ‘The Selfish Gene’ that “a molecule that makes copies of itself is not as difficult to imagine as it seems at first, and it only had to arise once.” Yes, just imagine. Given the immense complexity and technologies required for a cell to self-replicate, the idea of such a macro self-replicating machine arising spontaneously demands a great deal of imagination and a whole amount of luck. Eric H. Anderson captures this dilemma well:

“The accumulated evidence, taken together, strongly suggests that self-replication lies at the end of a very complicated, deeply integrated, highly sophisticated, thoughtfully planned, carefully controlled engineering process… The abiogenesis paradigm, with its placement of self-replication as the first stage of development, is fundamentally flawed at a conceptual level. It is opposed to both the evidence and our real-world experience and needs to be discarded.”²³

Conclusion—Beyond Naturalism

As I reach the end of this first section, I wonder if I have been truly fair? I admit to consciously playing devil’s advocate, and I’ve done so for a reason. The conventional narrative of life’s genesis—that neat, linear progression of chemical events—resonates as fundamentally incomplete. There is way more to the story, waiting to be told. The fact is, the prevailing narrative of abiogenesis tends to gloss over some uncomfortable truths, such that the debate around the origin of life is presented with a narrow bias, favouring naturalistic assumptions as the only scientifically acceptable perspective. I believe this presents a serious problem. We’ve inadvertently allowed a philosophical assumption, not arisen by science itself, to dictate the direction of what’s considered scientifically “acceptable” progress.

While we haven’t yet fully explored alternative theories, such as the RNA World Hypothesis, or the intricacies of molecular self-assembly (though we absolutely will), the central point is to illustrate that the field of chemical evolution is far from settled. To present it as a closed case is to oversimplify the ongoing debates—debates that, I would argue, challenge the very notion of biological life arising spontaneously.

Some prominent scientists are surprisingly frank about the challenges. Theoretical biologist Stuart Kauffman puts it bluntly: “Anyone who tells you that he or she knows how life started on the earth some 3.45 billion years ago is a fool or a knave. Nobody knows.”²⁴ Likewise, Jack W. Szostak, a Nobel laureate, stated that “It is virtually impossible to imagine how a cell’s machines, which are mostly protein-based catalysts called enzymes, could have formed spontaneously as life first arose from non-living matter… Thus, explaining how life began entails a serious paradox.”²⁵ George Whitesides, a Harvard chemist, admitted, “Most chemists believe, as do I, that life emerged spontaneously from mixtures of molecules in the prebiotic Earth. How? I have no idea… We need a really good new idea.”²⁶ Elsewhere, he states: “I don’t understand how you go from a system that’s random chemicals to something that becomes, in a sense, a Darwinian set of reactions that are getting more complicated spontaneously. I just don’t understand how that works.”²⁷ Antonio Lazcano, a renowned theoretician, noted in his Origin of Life entry in the Springer Encyclopedia of Astrobiology that: “A century and a half after Darwin admitted how little was understood about the origin of life, we still do not know when and how the first living beings appeared on Earth.”²⁸ James Tour provided a similar statement: “based on what we know of chemistry, life should not exist anywhere in the universe. Life’s ubiquity on this planet is utterly bizarre, and the lifelessness found on other planets makes far more chemical sense.”

So, what do we do with this uncertainty?

We acknowledge it. We accept that we need to broaden our perspective. For instance, consider discovering a nanotechnology device capable of generating energy, processing information, and fulfilling other essential functions. In any context apart from biology, we would likely view such complexity and efficiency as indicators of purposeful design. Observing the intricate structures and functions of cells, we often see what looks like signs of intentionality: foresight, coordination, and directed outcomes. According to our uniform experience, the presence of advanced organisation and abilities of living cells, would suggest some form of design. This perception could be an illusion—a point worth considering—or it might hint at a deeper truth.

For instance, consider this: if scientists were to build a cell from scratch in a lab, would that disprove intelligent design? Arguably, it would demonstrate the very principle—complex life requires intelligent assembly. Bringing the concept of intelligent design into discussions about the origins of life may seem unconventional, or taboo—especially within mainstream science, which tends to lean heavily on naturalistic assumptions. However, this isn’t about jumping to conclusions. Rather, it’s an opportunity to recognise the limits of our current knowledge, and therefore give ourselves permission to explore all sorts of other possibilities. Maybe that’ll lead us to a better, more satisfying story about how life began, though it may mean re-evaluating our assumptions. Of course, we still need to look at every idea with a critical eye. As we move to Part Two of this book, I simply ask that you consider these alternative ideas with an open mind, which doesn’t mean you have to necessarily accept them—just entertain them.

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