Semiquinone formation of d-amino-acid oxidase by irradiation

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-11-15 DOI:10.1016/0926-6593(66)90172-X

H. Watari, Kun-Joo Hwang, K. Ashida, K. Kinoshita

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引用次数: 6

Abstract

It has been found that oxidized d-amino-acid oxidase (d-amino-acid: oxygen oxidoreductase (deaminating), EC 1.4.3.3) is transformed to a semiquinone by irradiation with visible light. The semiquinone formation was detected by measurements of the optical absorption spectrum and electron spin resonance. A fairly stable semiquinone was obtained under anaerobic conditions but not under aerobic conditions since it easily reacted with molecular oxygen. After a cycle of semiquinone formation and reoxidation, the d-amino-acid oxidase activity was found to be completely restored. Although no evidence was obtained about an electron donor for the semiquinone formation, it did not appear likely, from the measurement of the activation energy of 5 kcal per mole, that water donated electrons. The electron spin resonance signal of the semiquinone exhibited an asymmetrical shape. Possible interpretations for the phenomena are discussed.

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辐照对d-氨基酸氧化酶半醌生成的影响

已发现氧化的d-氨基酸氧化酶(d-amino-acid: oxygen oxidoreductase (deamination)， EC 1.4.3.3)在可见光照射下转化为半醌。通过光学吸收光谱和电子自旋共振测量检测了半醌的形成。在厌氧条件下得到了相当稳定的半醌，而在好氧条件下则不能，因为它容易与分子氧反应。经过半醌形成和再氧化循环后，d-氨基酸氧化酶活性完全恢复。虽然没有证据表明半醌的形成有电子供体，但从每摩尔5千卡活化能的测量来看，似乎不太可能是水提供了电子。半醌的电子自旋共振信号呈不对称形状。对这些现象的可能解释进行了讨论。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation

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