title: Oxygen activation by cytochrome P450 monooxygenase.
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.
authors.affiliation: Department of Pharmacology, The University of Michigan, Ann Arbor, MI 48109, USA.
authors.forename: Djemel
authors.initials: D
authors.lastname: Hamdane
authors.forename: Haoming
authors.initials: H
authors.lastname: Zhang
authors.forename: Paul
authors.initials: P
authors.lastname: Hollenberg
mesh_terms: D003577:Cytochrome P-450 Enzyme System / Q000145:classification / Q000378:metabolism*; D004579:Electron Transport; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D011522:Protons; D014867:Water / Q000378:metabolism
chemical_list: D011522:Protons; D014867:Water; D003577:Cytochrome P-450 Enzyme System; D010100:Oxygen