Metal-carbon bonds in enzymes and cofactors / / edited by Astrid Sigel, Helmut Sigel, and Roland K.O. Sigel.
Saved in:
| Superior document: | Metal ions in life sciences, volume 6 |
|---|---|
| TeilnehmendeR: | |
| Place / Publishing House: | Cambridge, UK : : RSC Publishing,, 2009. |
| Year of Publication: | 2009 |
| Language: | English |
| Series: | Metal ions in life sciences ;
v. 6. |
| Online Access: | |
| Physical Description: | 1 online resource (532 pages) :; illustrations (some color). |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
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.