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Spin‐State Rationale for the Peroxo‐Stabilizing Role of the Thiolate Ligand in Superoxide Reductase
Author(s) -
Bukowski Michael R.,
Halfen Heather L.,
van den Berg Tieme A.,
Halfen Jason A.,
Que Lawrence
Publication year - 2005
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.200461527
Subject(s) - superoxide , ligand (biochemistry) , cleavage (geology) , chemistry , reductase , enzyme , spin states , bond cleavage , stereochemistry , spin (aerodynamics) , cytochrome c , crystallography , photochemistry , biochemistry , inorganic chemistry , materials science , mitochondrion , catalysis , physics , receptor , fracture (geology) , composite material , thermodynamics
Anti‐push : The axial thiolate ligand stabilizes high‐spin Fe III ‐OOR species (see picture) such as those found in superoxide reductase. This situation is in contrast to the “push effect” observed in structurally similar low‐spin Fe III ‐OOR systems, including cytochrome P450, which promote OO bond cleavage. These results show how very similar enzyme‐active sites can carry out two very different functions.