Metal-Carbon Bonds in Enzymes and Cofactors
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.
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
Sigel, Helmut
Sigel, Astrid
Sigel, Roland K. O.
| ISBN | 9783110442793 |
|---|---|
| Artikelnummer | 9783110442793 |
| Medientyp | Buch |
| Copyrightjahr | 2015 |
| Verlag | De Gruyter |
| Umfang | XX, 510 Seiten |
| Abbildungen | 50 b/w and 30 col. ill., 50 b/w tbl. |
| Sprache | Englisch |
