scholarly journals The Transformation by Catalysis of Prebiotic Chemical Systems to Useful Biochemicals: A Perspective Based on IR Spectroscopy of the Primary Chemicals II. Catalysis and the Building of RNA

2020 ◽  
Vol 10 (14) ◽  
pp. 4712
Author(s):  
Ragnar Larsson ◽  
Abdul Malek ◽  
Ingemar Odenbrand

Having found that carbonyl sulfide (COS), works well as a catalyst in the transformation of amino acids to polypeptides, we have now tested COS as a catalyst also for the formation of substances that might be thought of as partners in the building of RNA. The model used was selective energy transfer (SET). This model implies that a certain number of vibrational quanta are donated from the catalyst system and a corresponding number of quanta of the reactant accept the energy thus transferred. In this way, we found that carbonyl sulfide, COS, was a perfect catalyst for combining, first, five molecules of formaldehyde to form one molecule of ribose, and next, five molecules of hydrogen cyanide, HCN, to form one molecule of adenine, one of the nucleobases of RNA. However, beyond this, we found that COS was a perfect catalyst for precisely all reactions, needed to build the RNA, ribonucleic acid.

2020 ◽  
Vol 10 (3) ◽  
pp. 928 ◽  
Author(s):  
Ragnar Larsson ◽  
Abdul Malek

It is now widely speculated that life originated at the “Black Smokers” of the undersea hydrothermal vents, where conditions exist for the formation of the primary ingredients and their subsequent transformation to higher biotic species such as amino acids, alcohols, etc. Any possible routes for the prebiotic oligomerization of simple compounds like amino acids, necessary for cell formation, has so far not been well understood. However, Leman et al. recently reported that under standard laboratory conditions carbonyl sulfide (COS) can “mediate” the oligomerization of simple amino acids in moderate yield. COS being a well-known volcanic gas points to its possible role in prebiotic peptide formation in the environment of the hydrothermal vents. Based on a previously developed and tested model for selective (vibrational) energy transfer (SET), we show that a COS-catalyzed condensation of α-amino-acids can lead to the formation of polypeptides. We also indicate that other agents can act as catalysts of the amino acid condensation, such as Fe(CN)63− and cyanamide (H2N-CN). This is related to the existence of vibrations with a frequency near to that of the critical vibration of the reactant, ρw (NH2). This wagging vibration occurs at 1048 ± 10 cm−1 (the mean value of Cu and Ni complexes) and, as the vibration of the presumed catalyst lies at 2079 cm−1, one notes that one quantum of the catalyst equals two quanta of the NH2 wagging: 2079/2 × 1048 = 0.9919. This is a good indication of a resonance.


1997 ◽  
Vol 161 ◽  
pp. 179-187
Author(s):  
Clifford N. Matthews ◽  
Rose A. Pesce-Rodriguez ◽  
Shirley A. Liebman

AbstractHydrogen cyanide polymers – heterogeneous solids ranging in color from yellow to orange to brown to black – may be among the organic macromolecules most readily formed within the Solar System. The non-volatile black crust of comet Halley, for example, as well as the extensive orangebrown streaks in the atmosphere of Jupiter, might consist largely of such polymers synthesized from HCN formed by photolysis of methane and ammonia, the color observed depending on the concentration of HCN involved. Laboratory studies of these ubiquitous compounds point to the presence of polyamidine structures synthesized directly from hydrogen cyanide. These would be converted by water to polypeptides which can be further hydrolyzed to α-amino acids. Black polymers and multimers with conjugated ladder structures derived from HCN could also be formed and might well be the source of the many nitrogen heterocycles, adenine included, observed after pyrolysis. The dark brown color arising from the impacts of comet P/Shoemaker-Levy 9 on Jupiter might therefore be mainly caused by the presence of HCN polymers, whether originally present, deposited by the impactor or synthesized directly from HCN. Spectroscopic detection of these predicted macromolecules and their hydrolytic and pyrolytic by-products would strengthen significantly the hypothesis that cyanide polymerization is a preferred pathway for prebiotic and extraterrestrial chemistry.


ChemInform ◽  
1988 ◽  
Vol 19 (37) ◽  
Author(s):  
K. W. JUCKS ◽  
R. E. MILLER

1962 ◽  
Vol 48 (6) ◽  
pp. 1086-1092 ◽  
Author(s):  
F. Chapeville ◽  
F. Lipmann ◽  
G. v. Ehrenstein ◽  
B. Weisblum ◽  
W. J. Ray ◽  
...  
Keyword(s):  

1962 ◽  
Vol 40 (1) ◽  
pp. 653-666 ◽  
Author(s):  
Murray J. Fraser

A sensitive method for the measurement of amino acyl RNA synthetase activities (amino acid activating enzymes) is described. The method is based on measurements of the rates of labelling of soluble ribonucleic acid with14C-amino acids. Determinations of α-glutamyl-RNA, glutaminyl-RNA, and glycyl-RNA synthetase activities in the "pH 5 enzymes" fractions from rat liver and mouse Ehrlich ascites carcinoma cells have been made.


1969 ◽  
Vol 114 (2) ◽  
pp. 429-435 ◽  
Author(s):  
David J. Pillinger ◽  
John Hay ◽  
Ernest Borek

1. The ability of chemically hypermethylated Escherichia coli B transfer RNA to accept 19 amino acids was studied and the results were compared with those obtained with a control sample of E. coli B transfer RNA incubated under similar conditions in the absence of methylating agent. 2. There is a marked decrease in the ability of the modified transfer RNA to accept amino acids in almost all instances. 3. The acceptance of cysteine appears to be unique in that it is enhanced in the hypermethylated transfer RNA. 4. More detailed studies on the kinetics of acceptance for six amino acids is presented, emphasizing the variation in response of the individual amino acids. 5. Increasing hypermethylation causes a progressive decrease in the amino acid acceptance. 6. The results are discussed in terms of methylation at functional sites within the transfer RNA and possible conformational alterations to the structure of the macromolecule.


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