The problem with that being, that according to the research cited, the ambient pressure merely accelerates the decomposition of cytidine at the requisite temperatures. Indeed, the effects of pressure and temperature on organic molecules, is a problem not only faced by abiogenesis researchers, but medicinal chemists too. Finding ways of stopping this impacting a synthesis sometimes requires ingenuity in the med chem world.
Of course, as cited in that article, metal ion stabilisation could overcome this, but that's something else requiring empirical investigation, to see if it happens. If metal ion stabilisation doesn't happen, or is too weak in its effects to overcome the newly found additional destabilising effects of increased pressure at the temperatures in question, then that won't rescue the hypothesis.
Indeed, that's cited as the next project for the researchers - determine if metal ions in solution stabilise matters. Along with determining if coupling cytidine in a larger molecule stabilises matters. If the molecules you need, however, fall apart
quickly under the requisite conditions, then your mechanism starts to hit the buffers.
My own view is that the various hypotheses floating around for abiogenesis shouldn't be seen as
competitors, but as
contributors to the whole picture, with products from one mechanism helping another mechanism along. I suspect a
mature theory will eventually gravitate toward that view.
EDIT:
the paper itself drops another unfortunate problem into the mix, viz:
In this context, it must also be noted that although phosphodiester bonds have extreme chemical stability, with a half life for hydrolysis at 25°C and pH 7 of ~130,000 to 30,000,000 years,[13] in the presence of strong Lewis-acid species, featuring usually dizinc(II), dinickel(II) complexes or lanthanide species, hydrolysis rates are orders of magnitude higher than those for the deamination of cytosine.[14] Modern cytidine deaminases, including the APOBEC3 family of single-stranded DNA mutator proteins all feature a Zn(his)(cys)2 active site.[15].
Basically, that poses problems for the attachment of phosphate ions to one's nucleosides. The sugar-phosphate bond is remarkably resilient to hydrolysis - namely, being broken apart by the action of water. But that resilience decreases dramatically, the moment you have certain metal ions dissolved in the water in question. Ions such as Zn
2+, Ni
2+, La
3+, Ce
3+, etc., all speed up hydrolysis of the sugar-phosphate bond
enormously, depending upon concentration. As the paper states, an enzyme class specifically evolved for deamination of cytosine in specific circumstances, involves a Zn
2+ ion bolted onto the protein scaffold, and metal ions attached to proteins do a lot of chemical "heavy lifting" in the biosphere. But, that bolting of metal ions onto proteins, arises because the end result
controls the effect of the metal ion, and directs the metal ion's chemical reaction effects to a specific target. Free-moving metal ions in aqueous solution aren't subject to the same restrictions.
The entire pressure-temperature-pH space has long been known to exert effects upon reactions by chemists. Some reactions only vary modestly in reaction rate across wide variations of space parameters, whilst other reactions undergo dramatic changes of reaction rate.
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