Metal-carbon bonds in enzymes and cofactors /
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| Other Authors: | , , |
|---|---|
| Format: | Electronic eBook |
| Language: | English |
| Published: |
Cambridge, UK :
RSC Publishing,
2009.
|
| Series: | Metal ions in life sciences ;
v. 6. |
| Subjects: | |
| Online Access: | Click to View |
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Table of Contents:
- 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]-hydro-genases
- 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
- 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
- Reaction mechanism of the molybdenum hydroxylase xanthine oxidoreductase: evidence against the formation of intermediates having metal-carbon bonds.
