还原型纤维二糖氧化酶与氧气的反应。纤维二糖氧化酶主要是一种氧化酶吗？
Reactions of reduced cellobiose oxidase with oxygen. Is cellobiose oxidase primarily an oxidase?
作者信息
Wilson M T, Hogg N, Jones G D
机构信息
Department of Chemistry and Biological Chemistry, University of Essex, Colchester, U.K.
出版信息
Biochem J. 1990 Aug 15;270(1):265-7. doi: 10.1042/bj2700265.
Abstract
We report rapid-mixing experiments in which cellobiose oxidase, fully reduced with cellobiose, is allowed to react with excess molecular O2. Analysis of the progress curves and their comparison with computer simulations suggests that O2 reacts only with the cytochrome b-type haem and with a rate constant of approx. 0.5 s-1. In steady state the cytochrome b is partially oxidized, whereas the flavin remains largely reduced. This situation may be contrasted with that when dichloroindophenol is substituted for O2. Under these conditions the reactions are rapid (millisecond time range), and the redox centres in the enzyme appear to be oxidized simultaneously.
摘要
我们报告了快速混合实验，其中用纤维二糖完全还原的纤维二糖氧化酶与过量的分子氧反应。对反应进程曲线的分析以及与计算机模拟结果的比较表明，氧气仅与细胞色素b型血红素反应，反应速率常数约为0.5 s-1。在稳态下，细胞色素b被部分氧化，而黄素大部分仍保持还原状态。这种情况与用二氯靛酚代替氧气时的情况形成对比。在这些条件下，反应很快（毫秒时间范围），并且酶中的氧化还原中心似乎同时被氧化。
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本文引用的文献
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Resolution, purification and some properties of the multiple forms of cellobiose quinone dehydrogenase from the white-rot fungus Sporotrichum pulverulentum.粉状孢霉白腐真菌中纤维二糖醌脱氢酶多种形式的分离、纯化及某些性质
Biochem J. 1986 May 15;236(1):221-6. doi: 10.1042/bj2360221.
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Rapid kinetic studies of the reduction of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum by cellobiose.对来自白腐真菌粉状孢霉的纤维二糖氧化酶被纤维二糖还原的快速动力学研究。
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3
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Studies on the electron-transfer mechanism of the human neutrophil NADPH oxidase.人类中性粒细胞NADPH氧化酶电子转移机制的研究。
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