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Thiolate‐Bridged Iron–Nickel Models for the Active Site of [NiFe] Hydrogenase
Author(s) -
Ohki Yasuhiro,
Tatsumi Kazuyuki
Publication year - 2011
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201001087
Subject(s) - hydrogenase , nickel , active site , chemistry , catalysis , combinatorial chemistry , inorganic chemistry , biochemistry , organic chemistry
Hydrogenases catalyze the reversible oxidation of H 2 , which is crucial for the anaerobic metabolism of microorganisms. They attract growing interest in connection with H 2 ‐based energy systems. [NiFe] hydrogenase is the most common type among the currently known hydrogenases, and its active site consists of an “organometallic” Fe–Ni complex supported by cysteinyl thiolate ligands. This review presents an overview of the synthesis, properties, and reactions of thiolate‐bridged iron–nickel complexes that model the active site of [NiFe] hydrogenase.