Cytochrome P450–redox partner fusion enzymes

• Published in: Biochimica et biophysica acta Vol. 1770; no. 3; pp. 345 - 359
• Main Authors: Munro, Andrew W., Girvan, Hazel M., McLean, Kirsty J.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.03.2007
• Subjects: Amino Acid Sequence; Animals; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Binding Sites; Catalysis; Catalytic cycle; Chimera; Cytochrome P-450 Enzyme System - genetics; Cytochrome P-450 Enzyme System - metabolism; Cytochrome P450; Domain; Electron transfer; Electron Transport; Enzyme mechanism; Evolution, Molecular; Ferredoxin; Ferredoxins - genetics; Ferredoxins - metabolism; Flavodoxin; Flavoprotein; Fusion protein; Heme binding; Humans; Linker; Mixed Function Oxygenases - genetics; Mixed Function Oxygenases - metabolism; Models, Molecular; Molecular Sequence Data; NADP - metabolism; NADPH-Ferrihemoprotein Reductase - genetics; NADPH-Ferrihemoprotein Reductase - metabolism; Oxidation-Reduction; Oxygen - metabolism; Peroxidase; Phthalate dioxygenase reductase; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Redox partner; Cytochrome P450; Electron transfer; Flavoprotein; Linker; Redox partner; Heme binding; Enzyme mechanism; Flavodoxin; Peroxidase; Fusion protein; Ferredoxin; Domain; Phthalate dioxygenase reductase; Catalytic cycle; Chimera

The cytochromes P450 (P450s) are a broad class of heme b-containing mono-oxygenase enzymes. The vast majority of P450s catalyse reductive scission of molecular oxygen using electrons usually derived from coenzymes (NADH and NADPH) and delivered from redox partner proteins. Evolutionary advantages ma...