Metal-carbon bonds in enzymes and cofactors /

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Bibliographic Details
Other Authors: Sigel, Astrid (Editor), Sigel, Helmut (Editor), Sigel, Roland K. O. (Editor)
Format: Electronic eBook
Language:English
Published: Cambridge, UK : RSC Publishing, 2009.
Series:Metal ions in life sciences ; v. 6.
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Online Access:Click to View
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Table of Contents:
  • Organometallic chemistry of B12 coenzymes
  • Cobalamin- and corrinoid-dependent enzymes
  • Nickel-alkyl bond formation in the active site of methyl-coenzyme M reductase
  • Nickel-carbon bonds in acetyl-coenzyme a synthases/carbon monoxide dehydrogenases
  • Structure and function of [NiFe]-hydro-genases
  • Carbon monoxide and cyanide ligands in the active site of [FeFe]-hydrogenases
  • Carbon monoxide as intrinsic ligand to iron in the active site of [Fe]-hydrogenase
  • Dual role of heme as cofactor and substrate in the biosynthesis of carbon monoxide
  • Copper-carbon bonds in mechanistic and structural probing of proteins as well as in situations where copper is a catalytic or receptor site
  • Interaction of cyanide with enzymes containing vanadium, manganese, non-heme iron, and zinc
  • Reaction mechanism of the molybdenum hydroxylase xanthine oxidoreductase: evidence against the formation of intermediates having metal-carbon bonds.