title: Light-initiated hydroxylation of lauric acid using hybrid P450 BM3 enzymes.
abstract: We have developed hybrid P450 BM3 enzymes consisting of a Ru(II)-diimine photosensitizer covalently attached to non-native single cysteine residues of P450 BM3 heme domain mutants. These enzymes are capable, upon light activation, of selectively hydroxylating lauric acid with 40 times higher total turnover numbers compared to the peroxide shunt.
authors: San José State University, Department of Chemistry, One Washington Square, San José, CA 95192-0101, USA.
authors: Ngoc-Han
authors: NH
authors: Tran
authors: Ngoc
authors: N
authors: Huynh
authors: Thuba
authors: T
authors: Bui
authors: Yen
authors: Y
authors: Nguyen
authors: Phuong
authors: P
authors: Huynh
authors: Mary E
authors: ME
authors: Cooper
authors: Lionel E
authors: LE
authors: Cheruzel
mesh_terms: D019943:Amino Acid Substitution; D056831:Coordination Complexes / Q000737:chemistry; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics / Q000378:metabolism*; D006900:Hydroxylation; D007850:Lauric Acids / Q000737:chemistry / Q000378:metabolism*; D008027:Light; D009154:Mutation; D017319:Photosensitizing Agents / Q000737:chemistry; D012428:Ruthenium / Q000737:chemistry
chemical_list: D056831:Coordination Complexes; D007850:Lauric Acids; D017319:Photosensitizing Agents; C030358:lauric acid; D012428:Ruthenium; D003577:Cytochrome P-450 Enzyme System