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Formation of High‐Valent Iron–Oxo Species in Superoxide Reductase: Characterization by Resonance Raman Spectroscopy
Author(s) -
Bonnot Florence,
Tremey Emilie,
von Stetten David,
Rat Stéphanie,
Duval Simon,
Carpentier Philippe,
Clemancey Martin,
Desbois Alain,
Nivière Vincent
Publication year - 2014
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.201400356
Subject(s) - resonance raman spectroscopy , chemistry , superoxide , raman spectroscopy , active site , heme , coordination sphere , ferric , stereochemistry , enzyme , photochemistry , biochemistry , crystallography , inorganic chemistry , crystal structure , physics , optics
Superoxide reductase (SOR), a non‐heme mononuclear iron protein that is involved in superoxide detoxification in microorganisms, can be used as an unprecedented model to study the mechanisms of O 2 activation and of the formation of high‐valent iron–oxo species in metalloenzymes. By using resonance Raman spectroscopy, it was shown that the mutation of two residues in the second coordination sphere of the SOR iron active site, K 48 and I 118 , led to the formation of a high‐valent iron–oxo species when the mutant proteins were reacted with H 2 O 2 . These data demonstrate that these residues in the second coordination sphere tightly control the evolution and the cleavage of the OO bond of the ferric iron hydroperoxide intermediate that is formed in the SOR active site.