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Rapid, Reversible Oxygen Atom Transfer between an Oxomanganese( V ) Porphyrin and Bromide: A Haloperoxidase Mimic with Enzymatic Rates
Author(s) -
Jin Ning,
Bourassa James L.,
Tizio Steven C.,
Groves John T.
Publication year - 2000
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 - 10.1002/1521-3773(20001103)39:21<3849::aid-anie3849>3.0.co;2-0
Subject(s) - porphyrin , bromide , chemistry , oxygen atom , oxygen , atom (system on chip) , photochemistry , enzyme , myeloperoxidase , ion , inorganic chemistry , organic chemistry , molecule , biology , computer science , embedded system , immunology , inflammation
The oxygen atom donor ability of the oxomanganese( V ) porphyrin species 1 is comparable to that of myeloperoxidase compound I. This is one of the key findings of the reversible oxygen atom transfer reaction between 1 and bromide ion [Eq. (1)]. The well‐behaved equilibrium 1 ⇌ 2 allows definition of the free energy of the oxoMn V species.