Metal-Carbon Bonds in Enzymes and Cofactors (Metal Ions in Life Sciences 6) (2015. XX, 510 S. 50 b/w and 30 col. ill., 50 b/w tbl. 235 mm)

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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.

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.

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

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

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