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
Authors
Bibliographic Details
- 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
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:12759
- UUID:
-
uuid:c385a1f4-9623-4836-9150-47f0a978ca13
- Local pid:
- pubs:12759
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2009
If you are the owner of this record, you can report an update to it here: Report update to this record