Formation of High‐Valent Iron–Oxo Species in Superoxide Reductase: Characterization by Resonance Raman Spectroscopy1. Issue 23 (28th April 2014)

• Record Type: Journal Article
• Authors: Bonnot, Florence; Tremey, Emilie; von Stetten, David; Rat, Stéphanie; Duval, Simon; Carpentier, Philippe; Clemancey, Martin; Desbois, Alain; Nivière, Vincent
• Is Part Of: Angewandte Chemie international edition. Volume 53:Issue 23(2014)
• Page Start: 5926
• Page End: 5930
• Publication Date: 2014-04-28
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201400356
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>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 O₂ 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, K₄₈ and I₁₁₈, led to the formation of a high‐valent iron–oxo species when the mutant proteins were reacted with H₂O₂. These data demonstrate that these residues in the second coordination sphere tightly control the evolution and the cleavage of the OO bond of the ferric iron hydroperoxide intermediate that is formed in the SOR active site.</p> </abstract>