title: PHOTOCHEMICAL ACTION SPECTRUM OF THE TERMINAL OXIDASE OF MIXED FUNCTION OXIDASE SYSTEMS.
abstract: 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.
mesh_terms: 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
chemical_list: D000083:Acetanilides; D006908:Hydroxyprogesterones; D000632:Aminopyrine; D002248:Carbon Monoxide; D006899:Mixed Function Oxygenases; D010088:Oxidoreductases; D010105:Oxygenases; C508827:acetanilide; D003061:Codeine
keywords: ACETANILIDE; AMINOPYRINE; CARBON MONOXIDE; CODEINE; EXPERIMENTAL LAB STUDY; HYDROXYLASES; HYDROXYPROGESTERONE; LIGHT; LIVER ENZYMOLOGY; MICROSOMES; OXYGENASES; RATS