Document Type
Article
Language
eng
Format of Original
8 p.
Publication Date
6-9-2000
Publisher
Elsevier
Source Publication
Journal of Molecular Biology
Source ISSN
0022-2836
Original Item ID
doi: 10.1006/jmbi.2000.3702
Abstract
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 LIII-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.
Recommended Citation
Stewart, Lisa J.; Bailey, Susan; Bennett, Brian; Charnock, John M.; Garner, C. David; and McAlpine, Alan S., "Dimethylsulfoxide Reductase: An Enzyme Capable of Catalysis with Either Molybdenum or Tungsten at the Active Site" (2000). Physics Faculty Research and Publications. 84.
https://epublications.marquette.edu/physics_fac/84
Comments
Accepted version. Journal of Molecular Biology, Vol. 299, No. 3 (June 9, 2000): 593-600. DOI. © 2000 Elsevier. Used with permission.
Brian Bennett was affiliated with the CLRC Daresbury Laboratory Daresbury at the time of publication.