[Luminescent properties of NADPH: adrenodoxin reductase].
The fluorescent and phosphorescent properties of NADPH-adrenodoxin reductase were investigated. It was shown that the fluorescence of protein tryptophanyls was quenched completely by acrylamide and partially by ionic quenchers (I- and Cs+). A removal of the prosthetic group from the protein causes insignificant changes in fluorescent properties of the enzyme. The denaturation of the enzyme by urea was accompanied by growth of quenching parameters. Indeed, some differences were observed in the quenching of flavin fluorescence by ionic quenchers (I- and Cs+). NADPH appeared to be an efficient quencher of NADPH-adrenodoxin reductase tryptophan fluorescence. Using Förster's equations for non-radiative energy transfer, the distance between NADPH-binding site and tryptophanyls was evaluated to 35-40 A.
D020106:Acrylamide; D000178:Acrylamides / Q000494:pharmacology; D000302:Adrenal Cortex / Q000201:enzymology*; D000818:Animals; D001051:Apoenzymes / Q000032:analysis; D005287:Ferredoxin-NADP Reductase / Q000032:analysis*; D005182:Flavin-Adenine Dinucleotide / Q000494:pharmacology; D005453:Fluorescence; D008163:Luminescent Measurements; D008928:Mitochondria / Q000201:enzymology*; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis*; D011489:Protein Denaturation; D013696:Temperature; D014364:Tryptophan / Q000032:analysis; D014508:Urea / Q000494:pharmacology
D000178:Acrylamides; D001051:Apoenzymes; D005182:Flavin-Adenine Dinucleotide; D020106:Acrylamide; D014364:Tryptophan; D014508:Urea; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases
Liuminestsentnye svoĭstva NADPH: adrenodoksin reduktazy.