Haem-oxygen reactive intermediates: catalysis by the two-step

Author:

Makris T.M.1,Denisov I.G.2,Sligar S.G.123

Affiliation:

1. The Center for Biophysics and Computational Biology, University of Illinois Urbana-Champaign, 505 S. Goodwin Avenue, Urbana, IL 61801, U.S.A.

2. Departments of Biochemistry and Chemistry, University of Illinois Urbana-Champaign, 505 S. Goodwin Avenue, Urbana, IL 61801, U.S.A.

3. College of Medicine, University of Illinois Urbana-Champaign, 505 S. Goodwin Avenue, Urbana, IL 61801, U.S.A.

Abstract

The catalytic schemes of a variety of haem enzymes, including the P450 mono-oxygenases, consist of a number of common reactive haem-oxygen adducts. The characterization of these intermediates by optical and EPR spectroscopies has reinforced the similarity of these intermediate states in a number of haem enzyme systems. Furthermore, the reactivity of these states in P450 and horseradish peroxidase, in which multiple potent oxidants are formed, provides a paradigm for many other haem enzymes.

Publisher

Portland Press Ltd.

Subject

Biochemistry

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