First generation analogues of the binuclear site in the Fe-only hydrogenases: Fe{sub 2}({mu}-SR){sub 2}(CO){sub 4}(CN){sub 2}{sup 2{minus}}
Journal Article
·
· Journal of the American Chemical Society
Hydrogenase enzymes are utilized by numerous microorganisms to produce dihydrogen or to take up dihydrogen in support of their metabolic activities. The two families of metallo-hydrogenases feature FeM({mu}-SR){sub 2}(CO){sub n}(CN){sub n} cores. Having cyanide and CO coligands as well as metal-metal bonding, the hydrogenase active sites represent a link between the otherwise disparate realms of organometallic and biological Fe-S chemistry.
- Research Organization:
- Univ. of Illinois, Urbana, IL (US)
- Sponsoring Organization:
- USDOE; Alexander von Humboldt Foundation
- OSTI ID:
- 20013673
- Journal Information:
- Journal of the American Chemical Society, Vol. 121, Issue 41; Other Information: PBD: 20 Oct 1999; ISSN 0002-7863
- Country of Publication:
- United States
- Language:
- English
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