Formation of flavin semiquinone during the reduction of P450 BM3 reductase domain with NADPH.
Munro
A W
AW
Division of Biochemistry and Molecular Biology, University of Glasgow, U.K.
Coggins
J R
JR
Lindsay
J G
JG
Daff
S
S
Chapman
S K
SK
D001410:Bacillus megaterium / Q000201:enzymology; D001426:Bacterial Proteins; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism*; D005486:Flavin Mononucleotide / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism*; D019791:Guanidine; D006146:Guanidines; D006418:Heme / Q000378:metabolism; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D009251:NADPH-Ferrihemoprotein Reductase; D010084:Oxidation-Reduction; D011809:Quinones; D013053:Spectrophotometry
D001426:Bacterial Proteins; D006146:Guanidines; D011809:Quinones; D009243:NAD; D005182:Flavin-Adenine Dinucleotide; D006418:Heme; D005486:Flavin Mononucleotide; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases; D019791:Guanidine