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Unsaturated, Mixed‐Valence Diiron Dithiolate Model for the H ox State of the [FeFe] Hydrogenase
Author(s) -
Justice Aaron K.,
Rauchfuss Thomas B.,
Wilson Scott R.
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200702224
Subject(s) - hydrogenase , valence (chemistry) , chemistry , oxidation state , crystallography , valence electron , electronic structure , stereochemistry , computational chemistry , catalysis , electron , physics , quantum mechanics , biochemistry , organic chemistry
Chemists are closing in on functional and structural models for the [FeFe] hydrogenases. Oxidation of [Fe 2 (S 2 C 2 H 4 )(CO) 3 (PMe 3 )(dppv)] (dppv= cis ‐1,2‐C 2 H 2 (PPh 2 ) 2 ) by one electron affords a mixed‐valence model for the H ox state of the active site of the [FeFe] hydrogenases. Like the enzyme, this model exhibits the “rotated structure” and binds CO (see scheme). The radical character of the model is confirmed by its ready binding of NO.