MECHANISM OF ACTION OF XANTHINE-OXIDASE - RELATIONSHIP BETWEEN THE RAPID AND VERY RAPID MOLYBDENUM ELECTRON-PARAMAGNETIC-RESONANCE SIGNALS

被引：51

作者：

BRAY, RC ^{[1
]}

GUTTERIDGE, S ^{[1
]}

STOTTER, DA ^{[1
]}

TANNER, SJ ^{[1
]}

机构：

[1] UNIV ESSEX,DEPT CHEM,COLCHESTER CO4 3SQ,ESSEX,ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1979年 / 177卷 / 01期

关键词：

D O I：

10.1042/bj1770357

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：357 / 360

页数：4

共 16 条

[1] OXIDATION OF N-METHYL SUBSTITUTED HYPOXANTHINES, XANTHINES, PURINE-6,8-DIONES AND CORRESPONDING 6-THIOXO DERIVATIVES BY BOVINE MILK XANTHINE-OXIDASE [J].