期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 284, 期 32, 页码 21707-21718出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109.002709
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资金
- Biotechnology and Biological Sciences Research Council [P15195]
- Medical Research Council [G0400775]
- EPSRC [EP/D032210/1] Funding Source: UKRI
- MRC [G0400775] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/D032210/1] Funding Source: researchfish
- Medical Research Council [G0400775] Funding Source: researchfish
SoxB is an essential component of the bacterial Sox sulfur oxidation pathway. SoxB contains a di-manganese(II) site and is proposed to catalyze the release of sulfate from a protein-bound cysteine S-thiosulfonate. A direct assay for SoxB activity is described. The structure of recombinant Thermus thermophilus SoxB was determined by x-ray crystallography to a resolution of 1.5 angstrom. Structures were also determined for SoxB in complex with the substrate analogue thiosulfate and in complex with the product sulfate. A mechanistic model for SoxB is proposed based on these structures.
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