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The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures

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Abstract

Eight Ni proteins are known and three of these, CO dehydrogenase (CODH), acetyl-CoA synthase (ACS), and hydrogenase, are Ni-Fe-S proteins. In the last three years, the long-awaited structures of CODH and ACS have been solved. The bioinorganic community was shocked, as the structures of the active sites of CODH and ACS, the C- and A-cluster, respectively, which each had been predicted to consist of a [Fe4S4] cluster bridged to a single Ni, revealed unexpected compositions and arrangements. Crystal structures of ACS revealed major differences in protein conformation and in A-cluster composition; for example, a [Fe4S4] cluster bridged to a binuclear center in which one of the metal binding sites was occupied by Ni, Cu, or Zn. Recent studies have revealed Ni-Ni to be the active state, unveiled the source of the heterogeneity that had plagued studies of CODH/ACS for decades, and produced a metal-replacement strategy to generate highly active and nearly homogeneous enzyme.

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Abbreviations

CFeSP:

corrinoid iron-sulfur protein

CH3H4folate:

methyltetrahydrofolate

CODH/ACS:

carbon monoxide dehydrogenase/acetyl-CoA synthases

ENDOR:

electron nuclear double resonance

MeTr:

methyltransferase

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Acknowledgements

The authors gratefully acknowledge GM69857 for financial support.

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Authors and Affiliations

  1. Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA , 02139, USA

    Catherine L. Drennan

  2. Stanford Linear Accelerator Center, 2575 Sand Hill Road, MS99, Menlo Park, CA , 94025, USA

    Tzanko I. Doukov

  3. Department of Biochemistry, Beadle Center, University of Nebraska, Lincoln, NE , 68588-0664, USA

    Stephen W. Ragsdale

Authors
  1. Catherine L. Drennan
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  2. Tzanko I. Doukov
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  3. Stephen W. Ragsdale
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Correspondence to Catherine L. Drennan.

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Drennan, C.L., Doukov, T.I. & Ragsdale, S.W. The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures. J Biol Inorg Chem 9, 511–515 (2004). https://doi.org/10.1007/s00775-004-0563-y

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