P450-containing systems

Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.[1][2][3][4]

P450 enzymes usually function as a terminal oxidase in multicomponent electron-transfer chains, called P450-containing monooxygenase systems, although self-sufficient, non-monooxygenase P450s have been also described. All known P450-containing monooxygenase systems share common structural and functional domain architecture. Apart from the cytochrome itself, these systems contain one or more fundamental redox domains: FAD-containing flavoprotein or domain, FMN domain, ferredoxin and cytochrome b5. These ubiquitous redox domains, in various combinations, are widely distributed in biological systems. FMN domain, ferredoxin or cytochrome b5 transfer electrons between the flavin reductase (protein or domain) and P450. While P450-containing systems are found throughout all kingdoms of life, some organisms lack one or more of these redox domains.

  1. ^ Degtyarenko, K.N.; Kulikova, T.A. (2001). "Evolution of bioinorganic motifs in P450-containing systems". Biochem. Soc. Trans. 29 (2): 139–147. doi:10.1042/BST0290139. PMID 11356142.
  2. ^ Hanukoglu, I. (1996). "Electron transfer proteins of cytochrome P450 systems" (PDF). Adv. Mol. Cell Biol. Advances in Molecular and Cell Biology. 14: 29–56. doi:10.1016/S1569-2558(08)60339-2. ISBN 9780762301133.
  3. ^ McLean, K.J.; Sabri, M.; Marshall, K.R.; Lawson, R.J.; Lewis, D.G.; Clift, D.; Balding, P.R.; Dunford, A.J.; Warman, A.J.; McVey, J.P.; Quinn, A.-M.; Sutcliffe, M.J.; Scrutton, N.S.; Munro, A.W. (2005). "Biodiversity of cytochrome P450 redox systems". Biochem. Soc. Trans. 33 (4): 796–801. doi:10.1042/BST0330796. PMID 16042601.
  4. ^ Ohta, D.; Mizutani, M. (2004). "Redundancy or flexibility: molecular diversity of the electron transfer components for P450 monooxygenases in higher plants". Front. Biosci. 9 (1–3): 1587–1597. doi:10.2741/1356. PMID 14977570.