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. 1995 Oct 27;270(5236):628-30.
doi: 10.1126/science.270.5236.628.

A methylnickel intermediate in a bimetallic mechanism of acetyl-coenzyme A synthesis by anaerobic bacteria

M Kumar  1 , D Qiu, T G Spiro, S W Ragsdale
Affiliations

A methylnickel intermediate in a bimetallic mechanism of acetyl-coenzyme A synthesis by anaerobic bacteria

M Kumar et al. Science. .

Retraction in

  • Resonance Raman results.
    Spiro TG. Spiro TG. Science. 1997 Oct 3;278(5335):21. doi: 10.1126/science.278.5335.17h. Science. 1997. PMID: 9340748 No abstract available.

Abstract

Resonance Raman (RR) spectroscopy was used to identify a methylnickel adduct (upsilon Ni-C = 422 wave numbers) of carbon monoxide dehydrogenase (CODH) from Clostridium thermoaceticum. Formed at a nickel/iron-sulfur cluster on CODH called center A, the methylnickel species is the precursor of the methyl group of acetyl-coenzyme A in an anaerobic pathway of carbon monoxide or carbon dioxide fixation. Rapid kinetic and RR studies demonstrated that methylation of nickel occurs by heterolysis of the methyl-cobalt bond (upsilon Co-C = 429 wave numbers) of a methylated corrinoid/iron-sulfur protein. In combination with the earlier finding of an iron-carbonyl adduct at center A, detection of the methylnickel intermediate establishes a bimetallic mechanism for acetyl-coenzyme A synthesis.

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Comment in

  • Metal-carbon bonds in nature.
    Kovacs JA, Shoner SC, Ellison JJ. Kovacs JA, et al. Science. 1995 Oct 27;270(5236):587-8. doi: 10.1126/science.270.5236.587. Science. 1995. PMID: 7570015 Review. No abstract available.

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