Photosynthesis Research

, 98:657 | Cite as

Oxygen activation by cytochrome P450 monooxygenase

Review

Abstract

Unlike photosystem II (PSII) that catalyzes formation of the O–O bond, the cytochromes P450 (P450), members of a superfamily of hemoproteins, catalyze the scission of the O–O bond of dioxygen molecules and insert a single oxygen atom into unactivated hydrocarbons through a hydrogen abstraction-oxygen rebound mechanism. Hydroxylation of the unactivated hydrocarbons at physiological temperatures is vital for many cellar processes such as the biosynthesis of many endogenous compounds and the detoxification of xenobiotics in humans and plants. Even though it carries out the opposite of the water splitting reaction, P450 may share similarities to PSII in proton delivery networks, oxygen and water access channels, and consecutive electron transfer processes. In this article, we review recent advances in understanding the molecular mechanisms by which P450 activates dioxygen.

Keywords

P450 Oxygen intermediate Oxygen splitting Hydroxylation P450 reductase 

Abbreviations

P450

Cytochrome P450

cyt b5

Cytochrome b5

CPR

Cytochrome P450 reductase

Pdx

Putidaredoxin

Cpd I

Compound I

NADP

Nicotinamide adenine dinucleotide phosphate

PSII

Photosystem II

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Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  • Djemel Hamdane
    • 1
  • Haoming Zhang
    • 1
  • Paul Hollenberg
    • 1
  1. 1.Department of PharmacologyThe University of MichiganAnn ArborUSA

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