Premium
Synthetic Support of De Novo Design: Sterically Bulky [FeFe]‐Hydrogenase Models
Author(s) -
Singleton Michael L.,
Bhuvanesh Nattamai,
Reibenspies Joseph H.,
Darensbourg Marcetta Y.
Publication year - 2008
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.200803939
Subject(s) - steric effects , square pyramid , hydrogenase , ligand (biochemistry) , chemistry , active site , pyramid (geometry) , stereochemistry , crystallography , combinatorial chemistry , enzyme , mathematics , crystal structure , biochemistry , geometry , receptor
A twisted mimic : Upon oxidation of [(μ‐SCH 2 C(CH 3 ) 2 CH 2 S‐){Fe I (CO) 2 PMe 3 } 2 ], rearrangement yields the mixed‐valent Fe I Fe II cation in a square‐pyramid/inverted square‐pyramid geometry with a semibridging CO ligand, closely mimicking the [FeFe] hydrogenase enzyme active site. According to de novo design principles, the steric effect of bridgehead bulk in the S–S bridging ligand stabilizes this structure in the absence of the protein matrix.