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Oxygen activation by cytochrome P450 monooxygenase

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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.

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Fig. 1
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Scheme I

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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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  1. Department of Pharmacology, The University of Michigan, Ann Arbor, MI, 48109, USA

    Djemel Hamdane, Haoming Zhang & Paul Hollenberg

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  1. Djemel Hamdane
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  2. Haoming Zhang
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  3. Paul Hollenberg
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Correspondence to Haoming Zhang.

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Hamdane, D., Zhang, H. & Hollenberg, P. Oxygen activation by cytochrome P450 monooxygenase. Photosynth Res 98, 657–666 (2008). https://doi.org/10.1007/s11120-008-9322-1

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