ReviewBiochimica et biophysica acta2011
The cytochrome bd respiratory oxygen reductases.
Review in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 271 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
271 citing papers in PubMed, 1 synthesis or guideline pooled it, 511 citations in OpenAlex.
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- The role of cytochrome oxidases in bacterial virulence.Infection and immunity · 2026Review
- Electrogenic CH4 oxidation on a bioanode: putative extracellular electron transport system in Methylobacter sp.FEMS microbiology ecology · 2026Article
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- Oxygen reductase origin followed the great oxidation event and terminated the Lomagundi excursion.Biochimica et biophysica acta. Bioenergetics · 2026Article
- Energetics and Ecological Implications of Bacterial Electron Transport Chains.Environmental microbiology reports · 2026Review
- Investigating the role of cytochromeRSC medicinal chemistry · 2026Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Isolation and Characterization of a Novel Sulfur-OxidizingMicroorganisms · 2026Article
- A Novel Link Between Electron Transport Chain Modulation and mcl-PHA Production in Pseudomonas aeruginosa 5300 Using Azide as a Modulator.Environmental microbiology reports · 2026Article
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- Isolation of Allocrenothrix methanica reveals distinct ecophysiologies of filamentous methanotrophs and adaptations to O2 limitation.The ISME journal · 2026Article
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- Contrasting associations between microbiota respiratory strategies and seafloor macrofauna.ISME communications · 2026Article
- Sulphide and oleic acid synergism in accelerating mcl-PHA biopolymer production inBiochemistry and biophysics reports · 2025Article
- Ecogenomics and functional biogeography of the Roseobacter group in the global oceans based on 653 MAGs and SAGs.Microbiome · 2025Article
211 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
Cytochrome bd is a respiratory quinol: O₂ oxidoreductase found in many prokaryotes, including a number of pathogens. The main bioenergetic function of the enzyme is the production of a proton motive force by the vectorial charge transfer of protons. The sequences of cytochromes bd are not homologous to those of the other respiratory oxygen reductases, i.e., the heme-copper oxygen reductases or alternative oxidases (AOX). Generally, cytochromes bd are noteworthy for their high affinity for O₂ and resistance to inhibition by cyanide. In E. coli, for example, cytochrome bd (specifically, cytochrome bd-I) is expressed under O₂-limited conditions. Among the members of the bd-family are the so-called cyanide-insensitive quinol oxidases (CIO) which often have a low content of the eponymous heme d but, instead, have heme b in place of heme d in at least a majority of the enzyme population. However, at this point, no sequence motif has been identified to distinguish cytochrome bd (with a stoichiometric complement of heme d) from an enzyme designated as CIO. Members of the bd-family can be subdivided into those which contain either a long or a short hydrophilic connection between transmembrane helices 6 and 7 in subunit I, designated as the Q-loop. However, it is not clear whether there is a functional consequence of this difference. This review summarizes current knowledge on the physiological functions, genetics, structural and catalytic properties of cytochromes bd. Included in this review are descriptions of the intermediates of the catalytic cycle, the proposed site for the reduction of O₂, evidence for a proton channel connecting this active site to the bacterial cytoplasm, and the molecular mechanism by which a membrane potential is generated.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.