ArticleProceedings of the National Academy of Sciences of the United States of America2012
Mechanistic stoichiometry of proton translocation by cytochrome cbb3.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 36 citations in OpenAlex.
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- Electric fields control water-gated proton transfer in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Identification of nosZ-expressing microorganisms consuming trace NThe ISME journal · 2022Article
- Architecture of bacterial respiratory chains.Nature reviews. Microbiology · 2021Review
- Genes Linking Copper Trafficking and Homeostasis to the Biogenesis and Activity of theFrontiers in microbiology · 2021Article
- Molecular Hydrogen Metabolism: a Widespread Trait of Pathogenic Bacteria and Protists.Microbiology and molecular biology reviews : MMBR · 2020Review
- Respiratory Pathways Reconstructed by Multi-Omics Analysis inFrontiers in microbiology · 2017Article
- Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.Israel journal of chemistry · 2016Article
- The two transmembrane helices of CcoP are sufficient for assembly of the cbb3-type heme-copper oxygen reductase from Vibrio cholerae.Biochimica et biophysica acta · 2015Article
- Cytochrome cbb3 of Thioalkalivibrio is a Na+-pumping cytochrome oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Enzymatic characterization and in vivo function of five terminal oxidases in Pseudomonas aeruginosa.Journal of bacteriology · 2014Article
- The K(C) channel in the cbb3-type respiratory oxygen reductase from Rhodobacter capsulatus is required for both chemical and pumped protons.Journal of bacteriology · 2014Article
- Stoichiometry of proton pumping by the cbb3-type oxygen reductase in whole cells of Rhodobacter capsulatus at pH 7 is about 0.5 H+ per electron.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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3 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Cytochrome cbb(3) belongs to the superfamily of respiratory heme-copper oxidases that couple the reduction of molecular oxygen to proton translocation across the bacterial or mitochondrial membrane. The cbb(3)-type enzymes are found only in bacteria, and are both structurally and functionally the most distant from their mitochondrial counterparts. The mechanistic H(+)/e(-) stoichiometry of proton translocation in these cbb(3)-type cytochrome c oxidases has remained controversial. A stoichiometric efficiency of only one-half that of the mitochondrial aa(3)-type enzyme was recently proposed to be related to adaptation of the organism to microaerobic environments. Here, proton translocation by the Rhodobacter sphaeroides enzyme was studied using purified cytochrome cbb(3) reconstituted into liposomes. An H(+)/e(-) stoichiometry of proton translocation close to unity was observed using the oxygen pulse method, but solely in conditions in which the vast majority of the enzyme was fully reduced in the anaerobic state before the O(2) pulse. These data were compared with results using whole cells or spheroplasts, and the discrepancies in the literature data were discussed. Our results suggest that a proton-pumping efficiency of 1 H(+)/e(-) may be achieved using the single-proton uptake pathway identified in the structure of cytochrome cbb(3). The mechanism of proton pumping thus differs from that of the aa(3)-type oxidases of mitochondria and bacteria.
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