Dimethylsulfoxide reductase: An enzyme capable of catalysis with either molybdenum or tungsten at the active site

被引：93

作者：

Stewart, LJ

Bailey, S ^{[1
]}

Bennett, B

Charnock, JM

Garner, CD

McAlpine, AS

机构：

[1] CLRC, Daresbury Lab, Warrington WA4 4AD, Cheshire, England

[2] Univ Nottingham, Dept Chem, Nottingham NG7 2RD, England

[3] Univ Queensland, Dept Microbiol, Brisbane, Qld 4072, Australia

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2000年 / 299卷 / 03期

基金：

英国生物技术与生命科学研究理事会; 英国工程与自然科学研究理事会;

关键词：

dimethylsulfoxide reductase; tungsten; crystal structure; X-ray absorption spectroscopy (XAS); pyranopterin;

D O I：

10.1006/jmbi.2000.3702

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：

DMSO reductase (DMSOR) from Rhodobacter capsulatus, well-characterised as a molybdoenzyme, will bind tungsten. Protein crystallography has shown that tungsten in W-DMSOR is ligated by the dithiolene group of the two pyranopterins, the oxygen atom of Ser147 plus another oxygen atom, and is located in a very similar site to that of molybdenum in Mo-DMSOX. These conclusions are consistent with W L-III-edge X-ray absorption, EPR and UV/visible spectroscopic data. W-DMSOR is significantly more active than Mo-DMSOR in catalysing the reduction of DMSO but, in contrast to the latter, shows no significant ability to catalyse the oxidation of DMS. (C) 2000 Academic Press.

引用

页码：593 / 600

页数：8

共 37 条

[1] Reactions of dimethylsulfoxide reductase from Rhodobacter capsulatus with dimethyl sulfide and with dimethyl sulfoxide:: Complexities revealed by conventional and stopped-flow spectrophotometry [J].