I'm well familiar with Oro.
Here is my response to Oro:
If you want to understand the beginning of CELLULAR life, study lipids.
A stable cell membrane is the primary prerequisite for cellular life. It provides the compartmentation that supports evolution. Without it, all you have is a bunch of chemical reactions.
Lipids in isolation tend to form micelles, which are kind of like tiny soap bubbles except they're short lived because they get broken up by cations (calcium, magnesium, etc). The typical size of a micelle is a few hundred molecules, to understand what that means google "microsphere".
To get stable cell-type membranes you need PHOSPHO-lipids which increase cation resistance by orders of magnitude. Earth's early environment was anoxic and iron-rich, the first atmosphere was hydrogen sulfide. So you have to do that chemistry. When you do, the answer you get is GIANT membranes, with thousands of lipids.
Therefore, the isolated environment provided by these "cells" was very likely to contain the essential precursors for what we now know as cellular life - namely formamide, oxaloacetate, pyruvate, and so on - and you'll note that many of these are components of the Krebs cycle.
In the development of lipids, you want to pay attention to the transition between amphiphiles and full blown phospholipids. There are two kinds of phospholipids: phosphatidyls and sphingophospholipids. Phosphatidyls have a glycerol backbone with two acyl chains. In organic chemistry the classification is called Cahn-Ingold-Prelog. Cellular life uses phosphatidyls.
From there, it's relatively easy to map a pathway to simple cells like monococci. All you need is a cell wall and some transfer RNA. These are easily obtained in an anoxic iron rich environment with hydrogen sulfide, on the surface of clays - which are simply mixtures of dirt and water along with some volcanic ash and whatever organic material comes along for the ride. You WILL get fully enclosed phospholipid membranes under these conditions, and they WILL contain all the essential precursors for amino acids and nucleosides. Your pathway passes for example through the replacement of carboxyl groups by coenzyme A and then acetyl-coA, and suddenly this starts to sound like an introductory biochemistry class.
To get to an actual replicating cell you need additional compartments, which are easily created from invaginations of the outer membrane. The first need is simply a separate compartment where lipids can be synthesized. This gives you control over the size and layout of the cell. Notice we haven't invoked any RNA yet, all we have is membranes that bud off each other and recombine in various ways to form varying sized compartments, each of which contain a mix of various biomolecules.
The next step is to organize the mix. Before you can do that you need TRANSPORT across the membrane, so you can control what's in each compartment. This is most likely where proteins first come into play. The most primitive transporters are acyl carrier proteins, which are very small but contain the essential structure of a hydrophilic part and a hydrophobic part.
The protein chain formation from amino acids is actually very easy to explain, it's been done in the lab in a dozen different ways. See for example
Nucleic acids and polypeptides are at the heart of life. It is interesting to ask whether the monomers of these biopolymers possess intrinsic reactivity that favors oligomerization in the absence of enzymes. We have recently observed that covalently linked peptido RNA chains form when mixtures...
pubmed.ncbi.nlm.nih.gov
But keep in mind we're still talking about chemistry that can be achieved with iron and sulfur, and maybe a little copper and magnesium. To make your compartments useful, you need some complexity (some variation) in the lipid composition, you need various phosphate esters and so on. This evolution can occur in parallel with protein elongation, the two do not depend on each other.
To support useful life you need to get to the point where you have a compartment that synthesizes transmembrane proteins. (At this point still not under the guidance of nucleotides). Turns out that's pretty easy. When the protein is made inside the compartment, the first thing that happens is it tries to get out, and then it gets stuck in the membrane. Once that happens, a little bit of calcium will break off the piece of the membrane containing the protein. It'll turn into a "vesicle" - and basically this is the exact mechanism used by the endoplasmic reticulum of modern cells.
All of this is cut and dried, there's no question about any of it. These reactions have been replicated hundreds of times in the lab. By more than just biochemists - for example by organic chemists interested in the behaviors of surfactant and soap.
It’s exactly what I said - combinatorial explosion. These reactions and structures occur "because they can".