Redox Potentials of Glutaredoxins and Other Thiol-Disulfide Oxidoreductases of the Thioredoxin Superfamily Determined by Direct Protein-Protein Redox Equilibria
Open Access
- 1 December 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (49) , 30780-30786
- https://doi.org/10.1074/jbc.272.49.30780
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Glutaredoxin-3 from Escherichia coliPublished by Elsevier ,1996
- Electrostatic Interactions in the Active Site of the N-Terminal Thioredoxin-like Domain of Protein Disulfide IsomeraseBiochemistry, 1996
- Why is DsbA such an oxidizing disulfide catalyst?Cell, 1995
- A second class I ribonucleotide reductase in Enterobacteriaceae: characterization of the Salmonella typhimurium enzyme.Proceedings of the National Academy of Sciences, 1994
- Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant.Proceedings of the National Academy of Sciences, 1994
- Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductasesBiochemistry, 1993
- Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14.fwdarw.S) and its mixed disulfide with glutathioneBiochemistry, 1992
- Construction and characterization of glutaredoxin-negative mutants of Escherichia coli.Proceedings of the National Academy of Sciences, 1988
- Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathioneJournal of the American Chemical Society, 1980
- Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione.Proceedings of the National Academy of Sciences, 1976