Cytochrome P450 systems—biological variations of electron transport chains

• Published in: Biochimica et biophysica acta Vol. 1770; no. 3; pp. 330 - 344
• Main Authors: Hannemann, Frank, Bichet, Andreas, Ewen, Kerstin M., Bernhardt, Rita
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.03.2007
• Subjects: Animals; Biotransformation; Cytochrome P-450 Enzyme System - classification; Cytochrome P-450 Enzyme System - metabolism; Cytochrome P450; Electron transfer; Electron Transport; Heme-thiolate protein; Humans; Hydroxylation; Monooxygenase; Oxidation-Reduction; Oxygen - metabolism; P450 system; Pharmaceutical Preparations - metabolism; Redox partner; Xenobiotics - metabolism; Redox partner; Electron transfer; Heme-thiolate protein; P450 system; Monooxygenase; Cytochrome P450
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2006.07.017

Cytochromes P450 (P450) are hemoproteins encoded by a superfamily of genes nearly ubiquitously distributed in different organisms from all biological kingdoms. The reactions carried out by P450s are extremely diverse and contribute to the biotransformation of drugs, the bioconversion of xenobiotics, the bioactivation of chemical carcinogens, the biosynthesis of physiologically important compounds such as steroids, fatty acids, eicosanoids, fat-soluble vitamins and bile acids, the conversion of alkanes, terpenes and aromatic compounds as well as the degradation of herbicides and insecticides. Cytochromes P450 belong to the group of external monooxygenases and thus receive the necessary electrons for oxygen cleavage and substrate hydroxylation from different redox partners. The classical as well as the recently discovered P450 redox systems are compiled in this paper and classified according to their composition.