ArticleThe Journal of biological chemistry2014
How periplasmic thioredoxin TlpA reduces bacterial copper chaperone ScoI and cytochrome oxidase subunit II (CoxB) prior to metallation.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 42 citations in OpenAlex.
- CrpH ofFrontiers in microbiology · 2026Article
- Isolation, characterization, and genetic manipulation of cold-tolerant, manganese-oxidizingApplied and environmental microbiology · 2024Article
- Molecular Interactions of the Copper Chaperone Atx1 ofMicroorganisms · 2023Article
- The Escherichia coli MFS-type transporter genes yhjE, ydiM, and yfcJ are required to produce an active bo3 quinol oxidase.PloS one · 2023Article
- Diversity of CytochromeMicroorganisms · 2022Review
- The Role of COA6 in the Mitochondrial Copper Delivery Pathway to CytochromeBiomolecules · 2022Review
- The algal selenoproteomes.BMC genomics · 2020Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- Oxidative Stress-Generating Antimicrobials, a Novel Strategy to Overcome Antibacterial Resistance.Antioxidants (Basel, Switzerland) · 2020Review
- Search for Ancestral Features in Genomes ofGenes · 2019Article
- Biochemistry of Copper Site Assembly in Heme-Copper Oxidases: A Theme with Variations.International journal of molecular sciences · 2019Review
- Structural basis and mechanism for metallochaperone-assisted assembly of the CuScience advances · 2019Article
- Involvement of Glutaredoxin and Thioredoxin Systems in the Nitrogen-Fixing Symbiosis between Legumes and Rhizobia.Antioxidants (Basel, Switzerland) · 2018Review
- Characterization and effect of metal ions on the formation of the Thermus thermophilus Sco mixed disulfide intermediate.Protein science : a publication of the Protein Society · 2018Article
- The copper-deprivation stimulon ofThe Journal of biological chemistry · 2018Article
- A Copper Relay System Involving Two Periplasmic Chaperones Drives cbbACS chemical biology · 2018Article
- Mitochondrial cytochrome c oxidase biogenesis: Recent developments.Seminars in cell & developmental biology · 2018Review
- Structural analysis of human NHLRC2, mutations of which are associated with FINCA disease.PloS one · 2018Article
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8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two critical cysteine residues in the copper-A site (Cu(A)) on subunit II (CoxB) of bacterial cytochrome c oxidase lie on the periplasmic side of the cytoplasmic membrane. As the periplasm is an oxidizing environment as compared with the reducing cytoplasm, the prediction was that a disulfide bond formed between these cysteines must be eliminated by reduction prior to copper insertion. We show here that a periplasmic thioredoxin (TlpA) acts as a specific reductant not only for the Cu(2+) transfer chaperone ScoI but also for CoxB. The dual role of TlpA was documented best with high-resolution crystal structures of the kinetically trapped TlpA-ScoI and TlpA-CoxB mixed disulfide intermediates. They uncovered surprisingly disparate contact sites on TlpA for each of the two protein substrates. The equilibrium of CoxB reduction by TlpA revealed a thermodynamically favorable reaction, with a less negative redox potential of CoxB (E'0 = -231 mV) as compared with that of TlpA (E'0 = -256 mV). The reduction of CoxB by TlpA via disulfide exchange proved to be very fast, with a rate constant of 8.4 × 10(4) M(-1) s(-1) that is similar to that found previously for ScoI reduction. Hence, TlpA is a physiologically relevant reductase for both ScoI and CoxB. Although the requirement of ScoI for assembly of the Cu(A)-CoxB complex may be bypassed in vivo by high environmental Cu(2+) concentrations, TlpA is essential in this process because only reduced CoxB can bind copper ions.
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