EPR and X-ray crystallographic studies of dimethylsulfoxide reductase from Rhodobacter capsulatus: Implications for electron transfer and catalysis

Lane, Ian, Solomon, Peter S., Shaw, Anthony L., McAlpine, Alan S., Hanson, Graeme R., Bailey, Susan and McEwan, Alastair G. (1997). EPR and X-ray crystallographic studies of dimethylsulfoxide reductase from Rhodobacter capsulatus: Implications for electron transfer and catalysis. In: , Journal of Inorganic Biochemistry. Proceedings of: Eighth International Conference on Bioinorganic Chemistry. ICBIC 8: 8th International Conference on Bioinorganic Chemistry, Yokohama, Japan, (9-9). 27 July-1 August 1997.


Author Lane, Ian
Solomon, Peter S.
Shaw, Anthony L.
McAlpine, Alan S.
Hanson, Graeme R.
Bailey, Susan
McEwan, Alastair G.
Title of paper EPR and X-ray crystallographic studies of dimethylsulfoxide reductase from Rhodobacter capsulatus: Implications for electron transfer and catalysis
Formatted title EPR and X-ray crystallographic studies of dimethylsulfoxide reductase from Rhodobacter capsulatus: Implications for electron transfer and catalysis
Conference name ICBIC 8: 8th International Conference on Bioinorganic Chemistry
Conference location Yokohama, Japan
Conference dates 27 July-1 August 1997
Proceedings title Journal of Inorganic Biochemistry. Proceedings of: Eighth International Conference on Bioinorganic Chemistry   Check publisher's open access policy
Place of Publication New York, NY, U.S.A.
Publisher Elsevier
Publication Year 1997
DOI 10.1016/S0162-0134(97)89892-3
ISSN 0162-0134
1873-3344
Volume 67
Issue 1-4
Start page 9
End page 9
Total pages 1
Language eng
Formatted Abstract/Summary EPR spectroscopy in conjunction with isotope enrichment (95Mo, 2H and 17O) has been employed to probe the structure of the Mo(V) intermediates during catalysis.

We propose on the basis of our X-ray crystallographic data that the thiyl radical is centered on S1 of the Q-pterin which may be no longer coordinated to the Mo ion in the fully reduced structure. The ability to add one or more electrons to the Mo ion or the pterin suggests that the Q-pterin is involved in electron transfer between the native electron donor, cytochrome cdmso and MoCo in DMSO reductase. This hypothesis is strengthened by our observation of different redox states (fully oxidized and reduced) for the two pterins.
Subjects 0302 Inorganic Chemistry
030201 Bioinorganic Chemistry
Q-Index Code EX
Q-Index Status Provisional Code
Institutional Status Unknown
Additional Notes Published in Section (A) Molybedenum.

 
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Created: Tue, 20 Jul 2010, 10:21:13 EST by Jon Swabey on behalf of Faculty of Science