黄嘌呤氧化酶的作用机制。快速和极快速钼电子顺磁共振信号之间的关系。
The mechanism of action of xanthine oxidase. The relationship between the rapid and very rapid molybdenum electron-paramagnetic-resonance signals.
作者信息
Bray R C, Gutteridge S, Stotter D A, Tanner S J
出版信息
Biochem J. 1979 Jan 1;177(1):357-60. doi: 10.1042/bj1770357.
Abstract
On the basis of the work of Gutteridge, Tanner & Bray [Biochem. J. (1978) 175, 887-897] and of other data in the literature, a mechanism for the reaction of xanthine oxidase with reducing substrates is proposed. In the Michaelis complex, xanthine is bound to molybdenum via the N-9 nitrogen atom. Coupled transfer of two electrons to molybdenum and the C-8 proton to the enzyme yields (Enzyme)-Mo-SH. Concerted with this process, reaction of the xanthine residue with a nucleophile in the active centre yields a covalent intermediate that breaks down to give the product by alternative pathways at high and at low pH values.
摘要
基于古特里奇、坦纳和布雷的研究工作[《生物化学杂志》（1978年）175卷，887 - 897页]以及文献中的其他数据，提出了黄嘌呤氧化酶与还原性底物反应的机制。在米氏复合物中，黄嘌呤通过N - 9氮原子与钼结合。两个电子向钼的耦合转移以及C - 8质子向酶的转移产生（酶）- Mo - SH。与此过程协同进行的是，黄嘌呤残基与活性中心的亲核试剂反应生成共价中间体，该中间体在高pH值和低pH值下通过不同途径分解生成产物。
相似文献
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The mechanism of action of xanthine oxidase. The relationship between the rapid and very rapid molybdenum electron-paramagnetic-resonance signals.黄嘌呤氧化酶的作用机制。快速和极快速钼电子顺磁共振信号之间的关系。
Biochem J. 1979 Jan 1;177(1):357-60. doi: 10.1042/bj1770357.
2
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The mechanism of action of xanthine oxidase.黄嘌呤氧化酶的作用机制。
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The resolution of active and inactive xanthine oxidase by affinity chromatography.通过亲和色谱法分离活性和非活性黄嘌呤氧化酶。
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Catalysis of the direct transfer of oxygen from nicotinamide N-oxide to xanthine by xanthine oxidase.黄嘌呤氧化酶催化烟酰胺N-氧化物中的氧直接转移至黄嘌呤。
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Light-scattering studies on the action of endocellulases [proceedings].
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Comparison of the molybdenum centres of native and desulpho xanthine oxidase. The nature of the cyanide-labile sulphur atom and the nature of the proton-accepting group.天然型和脱硫型黄嘌呤氧化酶钼中心的比较。氰化物敏感硫原子的性质和质子接受基团的性质。
Biochem J. 1978 Dec 1;175(3):887-97. doi: 10.1042/bj1750887.
10
The molybdenum centre of native xanthine oxidase. Evidence for proton transfer from substrates to the centre and for existence of an anion-binding site.天然黄嘌呤氧化酶的钼中心。质子从底物转移至该中心以及存在阴离子结合位点的证据。
Biochem J. 1978 Dec 1;175(3):869-78. doi: 10.1042/bj1750869.
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