X-ray absorption spectroscopy of dimethyl sulfoxide reductase from Rhodobacter sphaeroides
- Stanford Univ., CA (United States)
- Duke Univ., Durham, NC (United States)
X-ray absorption spectroscopy at the molybdenum K-edge has been used to probe the molybdenum coordination of Rhodobacter sphaeroides dimethyl sulfoxide reductase. The molybdenum site of the oxidized protein possesses a novel Mo(VI) mono-oxo site (Mo=O at 1.68 A) with additional coordination by approximately four thiolate ligands at 2.44 A and probably one oxygen or nitogen at 1.92 A. The reduced Mo(IV) form of the enzyme is a des-oxomolybdenum with 3-4 thiolates at 2.33 A and two different Mo-O/N ligands at 2.16 A and 1.92 A. Similarly, the stable Mo(V) glycerol-inhibited species is found to be des-oxomolybdenum with approximately four thiolate ligands at 2.40 A and (probably) two similarly coordinated oxygen or nitrogen ligands at 1.96 A. 43 refs., 5 figs., 1 tab.
- OSTI ID:
- 219648
- Journal Information:
- Journal of the American Chemical Society, Vol. 118, Issue 5; Other Information: PBD: 7 Feb 1996
- Country of Publication:
- United States
- Language:
- English
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