期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 299, 期 3, 页码 593-600出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1006/jmbi.2000.3702
关键词
dimethylsulfoxide reductase; tungsten; crystal structure; X-ray absorption spectroscopy (XAS); pyranopterin
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.
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