Hemoproteins and related models in hydroxylation reactions of organic compounds Part I. Structure, function and catalytic activity of cytochrome P-450 and related models

P. Mohr*, F. Scheller, R. Renneberg, M. Kühn, K. Pommerening

*Corresponding author for this work

Research output: Contribution to journalJournal Articlepeer-review

4 Citations (Scopus)

Abstract

Cytochromes P-450 are widely spread in mammals, plants and microorganisms. These enzyme systems are able to catalyze chemical reactions of various organic compounds with molecular oxygen in a so-called mixed function oxidation reaction. All P-450 enzymes consist of an electron transfer component and a terminal oxidase with iron protoporphyrin IX as the prosthetic group. These enzyme systems also catalyze substrate conversion reactions of organic compounds by means of various hydroperoxides and H2O2, respectively. In spite of some similarities, the mechanisms of the H2O2-dependent reactions catalyzed by horse-radish peroxidase and P-450 differ significantly. On comparing the peroxide-dependent catalysis of P-450 and iron porphyrin complexes, however, a number of common characteristics have been analyzed.

Original languageEnglish
Pages (from-to)147-163
Number of pages17
JournalJournal of Molecular Catalysis
Volume13
Issue number2
DOIs
Publication statusPublished - Nov 1981
Externally publishedYes

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