X-ray absorption spectroscopy at the molybdenum K-edge has been used to probe the molybdenum coordination of Rhodobacter sphaeroides dimethylsulfoxide reductase. The molybdenum site of the oxidized protein possesses a novel Mo(VI) mono-oxo site (Mo=O at 1.68 w) with additional coordination by approximately four thiolate ligands at 2.44 w and probably one oxygen or nitrogen at 1.92 w. The reduced Mo(IV) form of the enzyme is a des-oxo molybdenum with 3-4 thiolates at 2.33 w and two different Mo_O/N ligands at 2.16 w and 1.92 w. Similarly, the stable Mo(V) glycerol-inhibited species is found to be a des-oxo molybdenum with approximately four thiolate ligands at 2.40 w and (probably) two similarly coordinated oxygen or nitrogen ligands at 1.96 w.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-17
Application #
5222837
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
17
Fiscal Year
1996
Total Cost
Indirect Cost
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