Flavin-dependent alcohol oxidase from the yeast Pichia pinus. Spatial localization of the coenzyme FAD in the protein structure: hot-tritium bombardment and ESR experiments.
The spatial localization of the coenzyme FAD in the quaternary structure of the alcohol oxidase from the yeast Pichia pinus was studied by tritium planigraphy and ESR methods. In the present paper we measured the specific radioactivity of FAD labelled as a part of the alcohol oxidase complex. The specific-radioactivity ratio for two FAD portions (FMN and AMP) was calculated. ESR experiments show 4 A (0.4 nm) to be the depth of immersion of paramagnetic isoalloxazines into alcohol oxidase octamer molecules. It is suggested that FAD molecules are bound to the surface of the octamer, rather than to the subunit interfaces. The orientation of the prosthetic group FAD in the alcohol oxidase protein is discussed.
Averbakh
A Z
AZ
Institute of Chemical Physics, Russian Academy of Sciences, Moscow Region.
Pekel
N D
ND
Seredenko
V I
VI
Kulikov
A V
AV
Gvozdev
R I
RI
Rudakova
I P
IP
D000249:Adenosine Monophosphate / Q000378:metabolism; D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D000465:Algorithms; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D005292:Ferricyanides / Q000494:pharmacology; D005486:Flavin Mononucleotide / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000032:analysis / Q000378:metabolism*; D007700:Kinetics; D010843:Pichia / Q000201:enzymology*; D011485:Protein Binding; D014316:Tritium
D005292:Ferricyanides; D014316:Tritium; D005182:Flavin-Adenine Dinucleotide; D000249:Adenosine Monophosphate; D005486:Flavin Mononucleotide; D000429:Alcohol Oxidoreductases; C019643:alcohol oxidase; C028033:potassium ferricyanide