A possible primordial peptide cycle
A possible primordial peptide cycle
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DOI：
10.1126/science.1086501
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发表时间：
2003-08-15
期刊：
影响因子：
56.9
通讯作者：
Wächtershäusher, G
中科院分区：
文献类型：
--
作者：
Huber, C;Eisenreich, W;Wächtershäusher, G
α-氨基酸可以通过在热的水性条件下在新鲜共沉淀的胶体（Fe，Ni）S存在下用一氧化碳（CO）活化而经历肽形成。我们现在表明，CO驱动的肽的形成进行伴随CO驱动的，N-末端肽降解外消旋N-末端乙内酰脲和尿素衍生物的α-氨基酸。这建立了一个肽循环与密切相关的合成代谢和分解代谢部分。乙内酰脲衍生物是嘌呤相关的杂环。（Fe，Ni）S依赖的尿素水解可能是镍酶尿素酶的进化前体。这些结果支持了化学自养起源的理论与CO驱动的，（Fe，Ni）S依赖的原始代谢。
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 nickel-enzyme urease. The results support the theory of a chemoautotrophic origin of life with a CO-driven, (Fe,Ni)S-dependent primordial metabolism.