Astrid Sigel & Helmut Sigel 
Metal-Carbon Bonds in Enzymes and Cofactors [PDF ebook] 

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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.

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Table of Content

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 [Ni Fe]-Hydrogenases
• Carbon Monoxide and Cyanide Ligands in the Active Site of [Fe Fe]-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

About the author

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

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Language English ● Format PDF ● Pages 530 ● ISBN 9783110436587 ● File size 59.8 MB ● Editor Astrid Sigel & Helmut Sigel ● Publisher De Gruyter ● City Berlin/Boston ● Published 2015 ● Edition 1 ● Downloadable 24 months ● Currency EUR ● ID 6586185 ● Copy protection Adobe DRM
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