X-ray absorption spectroscopy at the molybdenum and sulfur K-edges has been used to probe the active site of wild-type and cysteine 207 . serine mutant human sulfite oxidases. The active site structures of the oxidized (resting) Mo(VI) enzymes have been compared. The wild-type enzyme has been shown to possess two Mo=O ligands at 1.71 E and three Mo-S ligands at 2.41 E. The mutant enzyme possesses a novel tri-oxo molybdenum site with three Mo=O ligands at 1.74 E and two Mo-S ligands at 2.47 E. This work shows that cysteine 207 is a ligand of molybdenum in wild-type human sulfite oxidase, and that in the mutant the Mo is ligated to an extra oxo group rather than to the hydroxyl of the substituant serine 207. This work has been published: J. Am. Chem. Soc. 1996, 118, 8588-8592

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-23
Application #
6586759
Study Section
Project Start
2002-03-01
Project End
2003-02-28
Budget Start
Budget End
Support Year
23
Fiscal Year
2002
Total Cost
$143,176
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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