ArticleThe Journal of biological chemistry2011
Study of the thiol/disulfide redox systems of the anaerobe Desulfovibrio vulgaris points out pyruvate:ferredoxin oxidoreductase as a new target for thioredoxin 1.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 25 citations in OpenAlex.
- Text-Mining to Identify Gene Sets Involved in Biocorrosion by Sulfate-Reducing Bacteria: A Semi-Automated Workflow.Microorganisms · 2023Article
- When anaerobes encounter oxygen: mechanisms of oxygen toxicity, tolerance and defence.Nature reviews. Microbiology · 2021Review
- Structural and Biochemical Characterization of Thioredoxin-2 fromAntioxidants (Basel, Switzerland) · 2021Article
- Glutamate optimizes enzymatic activity under high hydrostatic pressure in Desulfovibrio species: effects on the ubiquitous thioredoxin system.Extremophiles : life under extreme conditions · 2021Article
- Unlocking Survival Mechanisms for Metal and Oxidative Stress in the Extremely Acidophilic, HalotolerantGenes · 2020Article
- Evolutionary adaptations that enable enzymes to tolerate oxidative stress.Free radical biology & medicine · 2019Review
- A Reexamination of Thioredoxin Reductase fromACS omega · 2017Article
- Biochemical Function, Molecular Structure and Evolution of an Atypical Thioredoxin Reductase fromFrontiers in microbiology · 2017Article
- A Novel F420-dependent Thioredoxin Reductase Gated by Low Potential FAD: A TOOL FOR REDOX REGULATION IN AN ANAEROBE.The Journal of biological chemistry · 2016Article
- Assessment of the Carbon Monoxide Metabolism of the Hyperthermophilic Sulfate-Reducing Archaeon Archaeoglobus fulgidus VC-16 by Comparative Transcriptome Analyses.Archaea (Vancouver, B.C.) · 2015Article
- Article
- Molecular cloning and characterization of a thioredoxin from Taiwanofungus camphorata.Botanical studies · 2014Article
- Hemerythrins in the microaerophilic bacterium Campylobacter jejuni help protect key iron-sulphur cluster enzymes from oxidative damage.Environmental microbiology · 2014Article
- Thioredoxin targets fundamental processes in a methane-producing archaeon, Methanocaldococcus jannaschii.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Ferredoxin:thioredoxin reductase (FTR) links the regulation of oxygenic photosynthesis to deeply rooted bacteria.Planta · 2013Article
- Structural and mechanistic insights into unusual thiol disulfide oxidoreductase.The Journal of biological chemistry · 2012Article
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9 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Sulfate reducers have developed a multifaceted adaptative strategy to survive against oxidative stresses. Along with this oxidative stress response, we recently characterized an elegant reversible disulfide bond-dependent protective mechanism in the pyruvate:ferredoxin oxidoreductase (PFOR) of various Desulfovibrio species. Here, we searched for thiol redox systems involved in this mechanism. Using thiol fluorescent labeling, we show that glutathione is not the major thiol/disulfide balance-controlling compound in four different Desulfovibrio species and that no other plentiful low molecular weight thiol can be detected. Enzymatic analyses of two thioredoxins (Trxs) and three thioredoxin reductases allow us to propose the existence of two independent Trx systems in Desulfovibrio vulgaris Hildenborough (DvH). The TR1/Trx1 system corresponds to the typical bacterial Trx system. We measured a TR1 apparent K(m) value for Trx1 of 8.9 μM. Moreover, our results showed that activity of TR1 was NADPH-dependent. The second system named TR3/Trx3 corresponds to an unconventional Trx system as TR3 used preferentially NADH (K(m) for NADPH, 743 μM; K(m) for NADH, 5.6 μM), and Trx3 was unable to reduce insulin. The K(m) value of TR3 for Trx3 was 1.12 μM. In vitro experiments demonstrated that the TR1/Trx1 system was the only one able to reactivate the oxygen-protected form of Desulfovibrio africanus PFOR. Moreover, ex vivo pulldown assays using the mutant Trx1(C33S) as bait allowed us to capture PFOR from the DvH extract. Altogether, these data demonstrate that PFOR is a new target for Trx1, which is probably involved in the protective switch mechanism of the enzyme.
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