Metal-carbon bonds in enzymes and cofactors  

 - Cambridge  RSC   2009 
 - xxvii, 510 p.   ill.  
 - Metal ions in life sciences, .
<br/><br/>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. 
<br/><br/><label>ISBN: </label>9781847559159 1847559158 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Metalloenzymes.<br/>Coenzymes.<br/>Organometallic compounds.<br/>Vitamin B12.<br/>Coenzymes<br/>Organometallic Compounds<br/>Multienzyme Complexes<br/>Oxidoreductases<br/>Vitamin B 12<br/>Cofaktor.<br/>Enzym.<br/>Metallorganische Verbindungen.
<br/><br/><label>LC Class. No.: </label>MED QP601.7  / M47