PHOTOCHEMICAL ACTION SPECTRUM OF THE TERMINAL OXIDASE OF MIXED FUNCTION OXIDASE SYSTEMS.
The reversal of the carbon monoxide inhibition by bands of monochromatic light was determined for the oxidative demethylation of codeine and monomethyl-4-aminopyrine and the hydroxylation of acetanilide by rat liver microsomes and for the hydroxylation of 17-hydroxyprogesterone at carbon-21 by bovine adrenocortical microsomes. Maximum reversal occurred at 450 millimicrons, the light absorption maximum of the CO compound of the CO-binding pigment of microsomes. The agreement between photochemical action spectrum and spectrophotometric difference spectrum supports the conclusion that the CO-binding pigment is the terminal oxidase of mixed function oxidase systems of mammals.
D000083:Acetanilides; D000632:Aminopyrine; D000818:Animals; D002248:Carbon Monoxide; D002417:Cattle; D003061:Codeine; D006900:Hydroxylation; D006908:Hydroxyprogesterones; D008027:Light; D008099:Liver / Q000201:enzymology*; D008861:Microsomes; D008862:Microsomes, Liver; D006899:Mixed Function Oxygenases; D010084:Oxidation-Reduction; D010088:Oxidoreductases; D010105:Oxygenases; D051381:Rats; D012106:Research
D000083:Acetanilides; D006908:Hydroxyprogesterones; D000632:Aminopyrine; D002248:Carbon Monoxide; D006899:Mixed Function Oxygenases; D010088:Oxidoreductases; D010105:Oxygenases; C508827:acetanilide; D003061:Codeine
ACETANILIDE; AMINOPYRINE; CARBON MONOXIDE; CODEINE; EXPERIMENTAL LAB STUDY; HYDROXYLASES; HYDROXYPROGESTERONE; LIGHT; LIVER ENZYMOLOGY; MICROSOMES; OXYGENASES; RATS