Metal-Carbon Bonds in Enzymes and Cofactors

The occurrence of a wide variety of metal-carbon bonds in living organisms, ranging from bacteria to humans, is only recently recognized. Of course, the historical examples are the B12 coenzymes containing cobalt-carbon bonds, but now such bonds are also known for nickel, iron, copper, and other transition metal ions. There is no other comparable book; MILS-6, written by 17 experts, summarizes the most recent insights into this fascinating topic.

Auteur

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

Contenu
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