Metal-Carbon Bonds in Enzymes and Cofactors

Helmut und Astrid Sigel, University of Basel, Switzerland. Roland K. O. Sigel, University of Zürich, Switzerland.

• From the Content:• 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]-Hydrogenases• 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• The 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• The Reaction Mechanism of the Molybdenum Hydroxylase Xanthine Oxidoreductase: Evidence Against the Formation of Intermediates Having Metal-Carbon Bonds• Computational Studies of Biooganometalllic Enzymes and Cofactors