Structural variability of the active site of Fe-only hydrogenase and its hydrogenated forms
- 1 January 1999
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Chemical Communications
- No. 17,p. 1655-1656
- https://doi.org/10.1039/a903803e
Abstract
Density functional calculations show that the (cys-S)- (CO)(CN)FeS2(µ-CO)Fe(CO)(CN) active site of the Fe-only hydrogenase from Clostridium pasteurianum is redox ambivalent and stereochemically flexible at the CO and S bridges, and at the Fe atoms, and with bound hydrogen: the fundamentals of probable mechanisms are revealed.Keywords
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