Flavocytochrome P450 BM3 and the origin of CYP102 fusion species. (25th October 2006)

• Record Type: Journal Article
• Authors: Girvan, H.M.; Waltham, T.N.; Neeli, R.; Collins, H.F.; McLean, K.J.; Scrutton, N.S.; Leys, D.; Munro, A.W.
• Is Part Of: Biochemical Society transactions. Volume 34:Number 6(2006)
• Page Start: 1173
• Page End: 1177
• Publication Date: 2006-10-25
• Subjects: Bacillus -- BM3 -- CYP102 -- electron transfer -- flavocytochrome -- haem; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0341173
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : Flavocytochrome P450 (cytochrome P450) BM3 is an intensively studied model system within the P450 enzyme superfamily, and is a natural fusion of a P450 to its P450 reductase redox partner. The fusion arrangement enables efficient electron transfer within the enzyme and a catalytic efficiency that cannot be matched in P450 systems from higher organisms. P450 BM3's potential for industrially relevant chemical transformations is now recognized, and variants with biotechnological applications have been constructed. Simultaneously, structural and mechanistic studies continue to reveal the intricate mechanistic details of this enzyme, including its dimeric organization and the relevance of this quaternary structure to catalysis. Homologues of BM3 have been found in several bacteria and fungi, indicating important physiological functions in these microbes and enabling first insights into evolution of the enzyme family. This short paper deals with recent developments in our understanding of structure, function, evolution and biotechnological applications of this important P450 system.