ArticleThe Journal of biological chemistry2010
Disparate pathways for the biogenesis of cytochrome oxidases in Bradyrhizobium japonicum.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 42 citations in OpenAlex.
- KLK8: charting new territories in left ventricular hypertrophy biomarker research.Biomarkers in medicine · 2025Article
- Mechanisms for Generating Low Potential Electrons across the Metabolic Diversity of Nitrogen-Fixing Bacteria.Applied and environmental microbiology · 2023Review
- Diversity of CytochromeMicroorganisms · 2022Review
- Effect of Copper on Expression of Functional Genes and Proteins Associated withInternational journal of molecular sciences · 2022Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- 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
- Expanding the Regulon of theFrontiers in microbiology · 2019Article
- An Integrated Systems Approach Unveils New Aspects of Microoxia-Mediated Regulation inFrontiers in microbiology · 2019Article
- A Copper Relay System Involving Two Periplasmic Chaperones Drives cbbACS chemical biology · 2018Article
- Article
- Cooperation between two periplasmic copper chaperones is required for full activity of the cbb3 -type cytochrome c oxidase and copper homeostasis in Rhodobacter capsulatus.Molecular microbiology · 2016Article
- How periplasmic thioredoxin TlpA reduces bacterial copper chaperone ScoI and cytochrome oxidase subunit II (CoxB) prior to metallation.The Journal of biological chemistry · 2014Article
- Copper starvation-inducible protein for cytochrome oxidase biogenesis in Bradyrhizobium japonicum.The Journal of biological chemistry · 2012Article
- The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb₃-type cytochrome oxidase in Rhodobacter capsulatus.Biochimica et biophysica acta · 2012Article
- Characterization of the PIB-Type ATPases present in Thermus thermophilus.Journal of bacteriology · 2012Article
- Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatus.Biochimica et biophysica acta · 2012Review
- The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidases.Biochimica et biophysica acta · 2012Article
- Bacterial adaptation of respiration from oxic to microoxic and anoxic conditions: redox control.Antioxidants & redox signaling · 2012Review
- The putative assembly factor CcoH is stably associated with the cbb3-type cytochrome oxidase.Journal of bacteriology · 2010Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This work addresses the biogenesis of heme-copper terminal oxidases in Bradyrhizobium japonicum, the nitrogen-fixing root nodule symbiont of soybean. B. japonicum has four quinol oxidases and four cytochrome oxidases. The latter include the aa(3)- and cbb(3)-type oxidases. Although both have a Cu(B) center in subunit I, the subunit II proteins differ in having either a Cu(A) center (in aa(3)) or a covalently bound heme c (in cbb(3)). Two biogenesis factors were genetically studied here, the periplasmically exposed CoxG and ScoI proteins, which are the respective homologs of the mitochondrial copper-trafficking chaperones Cox11 and Sco1 for the formation of the Cu(B) center in subunit I and the Cu(A) center in subunit II of cytochrome aa(3). We could demonstrate copper binding to ScoI in vitro, a process for which the thiols of cysteine residues 74 and 78 in the ScoI polypeptide were shown to be essential. Knock-out mutations in the B. japonicum coxG and scoI genes led to loss of cytochrome aa(3) assembly and activity in the cytoplasmic membrane, whereas the cbb(3)-type cytochrome oxidase apparently remained unaffected. This suggests that subunit I of the cbb(3)-type oxidase obtains its copper cofactor via a different pathway than cytochrome aa(3). In contrast to the coxG mutation, the scoI mutation caused a decreased symbiotic nitrogen fixation activity. We hypothesize that a periplasmic B. japonicum protein other than any of the identified Cu(A) proteins depends on ScoI and is required for an effective symbiosis.
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