Journal article icon

Journal article

Mechanism for the hydrolysis of a sulfur-sulfur bond based on the crystal structure of the thiosulfohydrolase SoxB.

Abstract:

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 A. Structures were also determined for SoxB in complex with the substrate analogue thiosulfate and in complex with the...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1074/jbc.m109.002709

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Expand authors...
Journal:
Journal of biological chemistry
Volume:
284
Issue:
32
Pages:
21707-21718
Publication date:
2009-08-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Source identifiers:
12759

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP