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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.
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Ian Dance (1999) studied this question.
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