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Science 15 August 2003:
Vol. 301. no. 5635, pp. 938 - 940
DOI: 10.1126/science.1086501
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Reports

A Possible Primordial Peptide Cycle

Claudia Huber,1 Wolfgang Eisenreich,1 Stefan Hecht,1 Günter Wächtershäuser2*

{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.

1 Department for Organic Chemistry and Biochemistry, Technische Universität München, Lichtenbergstraße 4, D-85747 Garching, Germany.
2 Department for Organic Chemistry and Biochemistry, Technische Universität München, Tal 29, D-80331 München, Germany.

* To whom correspondence should be addressed. E-mail: info{at}patent.de

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