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Frontispiece: Theory Uncovers the Role of the Methionine–Tyrosine–Tryptophan Radical Adduct in the Catalase Reaction of KatGs: O 2 Release Mediated by Proton‐Coupled Electron Transfer
Author(s) -
Wang Binju,
Fita Ignacio,
Rovira Carme
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201882069
Subject(s) - adduct , chemistry , catalase , electron transfer , reaction mechanism , covalent bond , hydrogen peroxide , metadynamics , photochemistry , stereochemistry , computational chemistry , enzyme , biochemistry , molecular dynamics , organic chemistry , catalysis
Nature has evolved a unique covalent M‐Y‐W adduct in the active site of catalase−peroxidase (KatGs) to catalyze the decomposition of exessive hydrogen peroxide through the catalase reaction, but the exact role of the adduct in this reaction was elusive up to now. Here, QM/MM calculations and QM/MM metadynamics simulations are employed to elucidate the molecular mechanism of the catalase reaction in KatGs. This study demonstrates that the M‐Y‐W adduct acts as an electron sink to mediate O 2 release via a novel proton‐coupled electron transfer mechanism. For more details see the Full Paper by C. Rovira et al. on page 5388 ff.