Metal-carbon bonds in enzymes and cofactors
Author(s)
Bibliographic Information
Metal-carbon bonds in enzymes and cofactors
(Metal ions in life sciences, v. 6)
Royal Society of Chemistry, c2009
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Note
Includes bibliographical references and index
Description and Table of Contents
Description
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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.
Table of Contents
- Chapter 1: ORGANOMETALLIC CHEMISTRY OF B12 COENZYMES
- Chapter 2: COBALAMIN- AND CORRINOID-DEPENDENT ENZYMES
- Chapter 3: NICKEL-ALKYL BOND FORMATION IN THE ACTIVE SITE OF METHYL-COENZYME M REDUCTASE
- Chapter 4: NICKEL-CARBON BONDS IN ACETYL-COENZYME A SYNTHASES/CARBON MONOXIDE DEHYDROGENASES
- Chapter 5: STRUCTURE AND FUNCTION OF [NiFe]-HYDROGENASES
- Chapter 6: CARBON MONOXIDE AND CYANIDE LIGANDS IN THE ACTIVE SITE OF [FeFe]-HYDROGENASES
- Chapter 7: CARBON MONOXIDE AS INTRINSIC LIGAND TO IRON IN THE ACTIVE SITE OF [Fe]-HYDROGENASE
- Chapter 8: THE DUAL ROLE OF HEME AS COFACTOR AND SUBSTRATE IN THE BIOSYNTHESIS OF CARBON MONOXIDE
- Chapter 9: COPPER-CARBON BONDS IN MECHANISTIC AND STRUCTURAL PROBING OF PROTEINS AS WELL AS IN SITUATIONS WHERE COPPER IS A CATALYTIC OR RECEPTOR SITE
- Chapter 10: INTERACTION OF CYANIDE WITH ENZYMES CONTAINING VANADIUM, MANGANESE, NON-HEME IRON, AND ZINC
- Chapter 11: THE REACTION MECHANISM OF THE MOLYBDENUM HYDROXYLASE XANTHINE OXIDOREDUCTASE: EVIDENCE AGAINST THE FORMATION OF INTERMEDIATES HAVING METAL-CARBON BONDS
- Chapter 12: COMPUTATIONAL STUDIES OF BIOORGANOMETALLIC ENZYMES AND COFACTORS
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