Abstract
alpha-Amino acids can undergo peptide formation by activation with carbon monoxide (CO) under hot aqueous conditions in the presence of freshly coprecipitated colloidal (Fe,Ni)S. We now show that CO-driven peptide formation proceeds concomitantly with CO-driven, N-terminal peptide degradation by racemizing N-terminal hydantoin and urea derivatives to alpha-amino acids. This establishes a peptide cycle with closely related anabolic and catabolic segments. The hydantoin derivative is a purin-related heterocycle. The (Fe,Ni)S-dependent urea hydrolysis could have been the evolutionary precursor of the nickelenzyme urease. The results support the theory of a chemoautotrophic origin of life with a CO-driven, (Fe,Ni)S-dependent primordial metabolism.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / chemistry
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Amino Acids / metabolism*
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Carbon Dioxide / chemistry
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Carbon Dioxide / metabolism
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Carbon Monoxide / chemistry
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Carbon Monoxide / metabolism*
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Chromatography, High Pressure Liquid
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Dipeptides / chemistry
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Dipeptides / metabolism
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Evolution, Chemical
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Ferrous Compounds / chemistry
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Ferrous Compounds / metabolism
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Hot Temperature
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Hydrogen-Ion Concentration
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Hydrolysis
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Mass Spectrometry
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Nickel / chemistry
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Nickel / metabolism
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Origin of Life*
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Oxidation-Reduction
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Peptides / chemistry
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Peptides / metabolism*
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Phenylalanine / chemistry
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Phenylalanine / metabolism*
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Pressure
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Stereoisomerism
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Urea / chemistry
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Urea / metabolism
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Urease / chemistry
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Urease / metabolism
Substances
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Amino Acids
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Dipeptides
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Ferrous Compounds
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Peptides
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Carbon Dioxide
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phenylalanylphenylalanine
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Phenylalanine
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Nickel
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Carbon Monoxide
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Urea
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Urease
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nickel sulfide
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ferrous sulfide