ArticleBiochemistry2010
The diheme cytochrome c(4) from Vibrio cholerae is a natural electron donor to the respiratory cbb(3) oxygen reductase.
Article in Biochemistry, 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, 36 citations in OpenAlex.
- Genetic potential for aerobic respiration and denitrification in globally distributed respiratory endosymbionts.Nature communications · 2024Article
- The structure of the diheme cytochrome cJournal of inorganic biochemistry · 2024Article
- Electrochemical and structural characterization of recombinant respiratory proteins of the acidophilic iron oxidizerFrontiers in microbiology · 2024Article
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Heterotrophic Sulfur Oxidation ofFrontiers in microbiology · 2022Article
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- Structure and redox properties of the diheme electron carrier cytochrome cJournal of inorganic biochemistry · 2020Article
- Mechanisms of Bacterial Tolerance and Persistence in the Gastrointestinal and Respiratory Environments.Clinical microbiology reviews · 2018Review
- Biphenyl Modulates the Expression and Function of Respiratory Oxidases in the Polychlorinated-Biphenyls DegraderFrontiers in microbiology · 2017Article
- Electron Accepting Units of the Diheme Cytochrome c TsdA, a Bifunctional Thiosulfate Dehydrogenase/Tetrathionate Reductase.The Journal of biological chemistry · 2016Article
- Delta-proteobacterial SAR324 group in hydrothermal plumes on the South Mid-Atlantic Ridge.Scientific reports · 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
- New Insight into Microbial Iron Oxidation as Revealed by the Proteomic Profile of an Obligate Iron-Oxidizing Chemolithoautotroph.Applied and environmental microbiology · 2015Article
- Conformational coupling between the active site and residues within the K(C)-channel of the Vibrio cholerae cbb3-type (C-family) oxygen reductase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A biochemical approach to study the role of the terminal oxidases in aerobic respiration in Shewanella oneidensis MR-1.PloS one · 2014Article
- The Herbaspirillum seropedicae SmR1 Fnr orthologs controls the cytochrome composition of the electron transport chain.Scientific reports · 2013Article
- Functional dissection of the multi-domain di-heme cytochrome c(550) from Thermus thermophilus.PloS one · 2013Article
- Product-controlled steady-state kinetics between cytochrome aa(3) from Rhodobacter sphaeroides and equine ferrocytochrome c analyzed by a novel spectrophotometric approach.Biochimica et biophysica acta · 2012Article
- Cytochrome c4 is required for siderophore expression by Legionella pneumophila, whereas cytochromes c1 and c5 promote intracellular infection.Microbiology (Reading, England) · 2011Article
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6 authors at 1 institution in 1 country.
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Abstract
The respiratory chain of Vibrio cholerae contains three bd-type quinol oxygen reductases as well as one cbb(3) oxygen reductase. The cbb(3) oxygen reductase has been previously isolated and characterized; however, the natural mobile electron donor(s) that shuttles electrons between the bc(1) complex and the cbb(3) oxygen reductase is not known. The most likely candidates are the diheme cytochrome c(4) and monoheme cytochrome c(5), which have been previously shown to be present in the periplasm of aerobically grown cultures of V. cholerae. Both cytochromes c(4) and c(5) from V. cholerae have been cloned and expressed heterologously in Escherichia coli. It is shown that reduced cytochrome c(4) is a substrate for the purified cbb(3) oxygen reductase and can support steady state oxygen reductase activity of at least 300 e(-1)/s. In contrast, reduced cytochrome c(5) is not a good substrate for the cbb(3) oxygen reductase. Surprisingly, the dependence of the oxygen reductase activity on the concentration of cytochrome c(4) does not exhibit saturation. Global spectroscopic analysis of the time course of the oxidation of cytochrome c(4) indicates that the apparent lack of saturation is due to the strong dependence of K(M) and V(max) on the concentration of oxidized cytochrome c(4). Whether this is an artifact of the in vitro assay or has physiological significance remains unknown. Cyclic voltammetry was used to determine that the midpoint potentials of the two hemes in cytochrome c(4) are 240 and 340 mV (vs standard hydrogen electrode), similar to the electrochemical properties of other c(4)-type cytochromes. Genomic analysis shows a strong correlation between the presence of a c(4)-type cytochrome and a cbb(3) oxygen reductase within the beta- and gamma-proteobacterial clades, suggesting that cytochrome c(4) is the likely natural electron donor to the cbb(3) oxygen reductases within these organisms. These would include the beta-proteobacteria Neisseria meningitidis and Neisseria gonnorhoeae, in which the cbb(3) oxygen reductases are the only terminal oxidases in their respiratory chains, and the gamma-proteobacterium Pseudomonas stutzeri.
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