辐照对d-氨基酸氧化酶半醌生成的影响

H. Watari, Kun-Joo Hwang, K. Ashida, K. Kinoshita
{"title":"辐照对d-氨基酸氧化酶半醌生成的影响","authors":"H. Watari,&nbsp;Kun-Joo Hwang,&nbsp;K. Ashida,&nbsp;K. Kinoshita","doi":"10.1016/0926-6593(66)90172-X","DOIUrl":null,"url":null,"abstract":"<div><p>It has been found that oxidized <span>d</span>-amino-acid oxidase (<span>d</span>-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 <span>d</span>-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.</p></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 2","pages":"Pages 256-261"},"PeriodicalIF":0.0000,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90172-X","citationCount":"6","resultStr":"{\"title\":\"Semiquinone formation of d-amino-acid oxidase by irradiation\",\"authors\":\"H. Watari,&nbsp;Kun-Joo Hwang,&nbsp;K. Ashida,&nbsp;K. Kinoshita\",\"doi\":\"10.1016/0926-6593(66)90172-X\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>It has been found that oxidized <span>d</span>-amino-acid oxidase (<span>d</span>-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 <span>d</span>-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.</p></div>\",\"PeriodicalId\":100160,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"volume\":\"128 2\",\"pages\":\"Pages 256-261\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1966-11-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6593(66)90172-X\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/092665936690172X\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/092665936690172X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 6

摘要

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。
Semiquinone formation of d-amino-acid oxidase by irradiation

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.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信