X-ray absorption spectroscopy of dimethyl sulfoxide reductase from Rhodobacter sphaeroides

被引:116
作者
George, GN [1 ]
Hilton, J [1 ]
Rajagopalan, KV [1 ]
机构
[1] DUKE UNIV, SCH MED, DEPT BIOCHEM, DURHAM, NC 27710 USA
关键词
D O I
10.1021/ja953317l
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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-ore site (Mo=O at 1.68 Angstrom) with additional coordination by approximately four thiolate ligands at 2.44 Angstrom and probably one oxygen or nitrogen at 1.92 Angstrom. The reduced Mo(IV) form of the enzyme is a des-oxomolybdenum with 3-4 thiolates at 2.33 Angstrom and two different Mo-O/N ligands at 2.16 Angstrom and 1.92 Angstrom. Similarly, the stable Mo(V) glycerol-inhibited species is found to be a des-oxomolybdenum with approximately four thiolate ligands at 2.40 Angstrom and (probably) two similarly coordinated oxygen or nitrogen ligands at 1.96 Angstrom.
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页码:1113 / 1117
页数:5
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