Interaction of arsenate with the molybdenum site of sulfite oxidase

Journal of the American Chemical Society

Volumn 120, Issue 18, 1998, Pages 4522-4523

  George, Graham N ^a   Garrett, Robert M ^b   Graf, Tyler ^b   Prince, Roger C ^c   Rajagopalan, K V ^b  

^a SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^b DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c EXXONMOBIL UPSTREAM RESEARCH COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0001693415     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja973473n     Document Type: Letter

References (36)

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13. EPR spectroscopy used a Varian E109 instrument, with 0.1-mT modulation amplitude, 10-mW applied power, and the sample at 150 K. Recombinant human sulfite oxidase was purified as previously described (Garrett, R. M.; Rajagopalan, K. V. J. Biol. Chem. 1996, 271, 7387-7391). Samples for EPR spectroscopy and for XAS (0.1 and 0.5 mM Mo, respectively) in 50 mM bis-tris- propane buffer at pH 6.5 were reduced with 1 mM sulfite for 30 s.
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34. Refinements including an additional. Mo-O yielded very large DebyeWaller factors that effectively removed this Mo-O EXAFS.
35. George, G. N., Garrett, R. M.; Graf, T.; Prince, R. C.; Rajagopalan K. V. Unpublished work.
36. Formation of a monodentate sulfate complex might proceed via a bidentate intermediate if sulfite is directly coordinated to molybdenum in the Michaelis complex.