Flavocytochrome P450 BM3 substrate selectivity and electron transfer in a model cytochrome P450.
Munro
A W
AW
Department of Pure & Applied Chemistry, University of Strathclyde, Royal College, 204 George St., Glasgow, G1 1XL, UK.
Noble
M A
MA
Ost
T W
TW
Green
A J
AJ
McLean
K J
KJ
Robledo
L
L
Miles
C S
CS
Murdoch
J
J
Chapman
S K
SK
D000818:Animals; D001426:Bacterial Proteins; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004579:Electron Transport; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008956:Models, Chemical; D016297:Mutagenesis, Site-Directed; D009251:NADPH-Ferrihemoprotein Reductase; D011487:Protein Conformation; D013379:Substrate Specificity
D001426:Bacterial Proteins; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases