The Thioredoxin Domain of Neisseria gonorrhoeae PilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases
Open Access
- 1 October 2006
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 281 (43) , 32668-32675
- https://doi.org/10.1074/jbc.m604971200
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- The N-terminal Domain of PILB from Neisseria meningitidis Is a Disulfide Reductase That Can Recycle Methionine Sulfoxide ReductasesJournal of Biological Chemistry, 2005
- Methionine sulfoxide reductases in prokaryotesBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2005
- Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damagePublished by Elsevier ,2004
- The enzymology and biochemistry of methionine sulfoxide reductasesBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2004
- Kinetic Characterization of the Catalytic Mechanism of Methionine Sulfoxide Reductase B from Neisseria meningitidisBiochemistry, 2004
- Kinetic Characterization of the Chemical Steps Involved in the Catalytic Mechanism of Methionine Sulfoxide Reductase A from Neisseria meningitidisJournal of Biological Chemistry, 2003
- The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen speciesProceedings of the National Academy of Sciences, 2002
- Crystal Structure of the Escherichia coli Peptide Methionine Sulphoxide Reductase at 1.9 Å ResolutionStructure, 2000
- Structure and Mechanism of Peptide Methionine Sulfoxide Reductase, an “Anti-Oxidation” Enzyme,Biochemistry, 2000
- Thiol–disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductaseProceedings of the National Academy of Sciences, 2000