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

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
C L DrennanS W Ragsdale

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 [Fe(4)S(4)] 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 [Fe(4)S(4)] 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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Citations

Aug 10, 2010·Journal of Industrial Microbiology & Biotechnology·Jyotisna Saxena, Ralph S Tanner
Sep 14, 2006·Journal of the American Chemical Society·Xiangshi TanPaul A Lindahl
Dec 3, 2009·Journal of the American Chemical Society·Sheel C DodaniChristopher J Chang
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