Some Physico-chemical Properties of the Photo-induced Semiquinone of D-Amino Acid Oxidase and Influence of Pyruvate and Phenylpyruvate upon Its Formation
- 1 April 1967
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 61 (4) , 433-439
- https://doi.org/10.1093/oxfordjournals.jbchem.a128566
Abstract
1. The absorption spectrum of the photo-induced semiquinone of D-amino acid oxidase [EC 1.4.3.3] was calculated. The spectrum coincided with that of the dithionite reduced semiquinone. 2. The E′o of photo-induced semiquinone was estimated as approximately—-125 mV. The semiquinone reduced cytochrome c in an anaerobic condition. 3. D-Amino acid oxidase combined with pyruvate or phenylpyruvate did not form the photo-induced semiquinone by irradiation under anaerobic conditions, but turned to colorless form. This colorless form was not autoxidizablc and contained undecomposed flavin.This publication has 5 references indexed in Scilit:
- An electron spin resonance study of the semiquinonoid state of d-amino acid oxidaseArchives of Biochemistry and Biophysics, 1964
- Semiquinone and Enzyme Kinetics of D-Amino Acid OxidaseThe Journal of Biochemistry, 1963
- Complex formation of apo-enzyme, coenzyme and substrate of d-amino acid oxidaseBiochimica et Biophysica Acta, 1962
- The purification and some properties of d-amino acid oxidaseBiochimica et Biophysica Acta, 1961
- Photochemical oxidation and reduction reactions catalyzed by flavin nucleotidesBiochimica et Biophysica Acta, 1959