1e18: Difference between revisions
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Revision as of 12:59, 30 October 2007
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TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS
Overview
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-DMSOR. 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.
About this Structure
1E18 is a [Single protein] structure of sequence from [Rhodobacter capsulatus] with PGD, 6WO and EOH as [ligands]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site., Stewart LJ, Bailey S, Bennett B, Charnock JM, Garner CD, McAlpine AS, J Mol Biol. 2000 Jun 9;299(3):593-600. PMID:10835270
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