Active sites of transition-metal enzymes with a focus on nickel

Citation
U. Ermler et al., Active sites of transition-metal enzymes with a focus on nickel, CURR OP STR, 8(6), 1998, pp. 749-758
Citations number
98
Categorie Soggetti
Biochemistry & Biophysics
Journal title
CURRENT OPINION IN STRUCTURAL BIOLOGY
ISSN journal
0959440X → ACNP
Volume
8
Issue
6
Year of publication
1998
Pages
749 - 758
Database
ISI
SICI code
0959-440X(199812)8:6<749:ASOTEW>2.0.ZU;2-S
Abstract
Since 1995, crystal structures have been determined for many transition-met al enzymes, in particular those containing the rarely used transition metal s vanadium, molybdenum, tungsten, manganese, cobalt and nickel. Accordingly , our understanding of how an enzyme uses the unique properties of a specif ic transition metal has been substantially increased in the past few years. The different functions of nickel in catalysis are highlighted by describi ng the active sites of six nickel enzymes - methyl-coenyzme M reductase, ur ease, hydrogenase, superoxide dismutase, carbon monoxide dehydrogenase and acetyl-coenzyme A synthase.