The DOI matches its Crossref record; 98 of the 98 references it cites were found in a registry or an index.
The Protonmotive Q Cycle in Mitochondria and Bacteria
Abstract
The cytochrome bc1 complex is an oligomeric electron transfer enzyme located in the inner membrane of mitochondria and the plasma membrane of bacteria. The cytochrome bc1 complex participates in respiration in eukaryotic cells and also participates in respiration, cyclic photosynthetic electron transfer, denitrification, and nitrogen fixation in a phylogenetically diverse collection of bacteria. In all of these organisms, the cytochrome bc1 complex transfers electrons from ubiquinol to cytochrome c and links this electron transfer to translocation of protons across the membrane in which it resides, thus converting the available free energy of the oxidation-reduction reaction into an electrochemical proton gradient. The mechanism by which the cytochrome bc1 complex achieves this energy transduction is the protonmotive Q cycle. The Q cycle mechanism has been documented by extensive experimentation, and recent investigations have focused on structural features of the three redox subunits of the bc1 complex essential to the protonmotive and electrogenic activities of this membranous enzyme.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
MITCHELL, P. (1961) · Nature · doi:10.1038/191144a0 · Cited by 4,704
Deisenhofer, J., Epp, O., Miki, K., Huber, R., & Michel, H. (1985) · Nature · doi:10.1038/318618a0 · Cited by 3,068
Anoxygenic Photosynthetic Bacteria
(1995) · Advances in Photosynthesis and Respiration · doi:10.1007/0-306-47954-0 · Cited by 1,902
Nature of biological electron transfer
Moser, C. C., Keske, J. M., Warncke, K., Farid, R. S., & Dutton, P. L. (1992) · Nature · doi:10.1038/355796a0 · Cited by 1,880
Possible molecular mechanisms of the protonmotive function of cytochrome systems
Mitchell, P. (1976) · Journal of Theoretical Biology · doi:10.1016/0022-5193(76)90124-7 · Cited by 1,268
The protonmotive Q cycle: A general formulation
Mitchell, P. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80359-0 · Cited by 624
Trumpower, B. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38410-8 · Cited by 595
Self-citationMitchell, P. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80098-6 · Cited by 441
Widger, W. R., Cramer, W. A., Herrmann, R. G., & Trebst, A. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.3.674 · Cited by 401
Mitochondrial cytochrome b: evolution and structure of the protein
Esposti, M. D., De Vries, S., Crimi, M., Ghelli, A., Patarnello, T., & Meyer, A. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90197-n · Cited by 398
Cited by
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253
Buckel, W., & Thauer, R. K. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.07.002 · Cited by 797
The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex
Dröse, S., & Brandt, U. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803236200 · Cited by 386
Self-citationSuperoxide generation by complex III: From mechanistic rationales to functional consequences
Bleier, L., & Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.12.002 · Cited by 369
Sousa, F. L., Thiergart, T., Landan, G., Nelson-Sathi, S., Pereira, I. A. C., Allen, J. F., Lane, N., & Martin, W. F. (2013) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0088 · Cited by 286
Metadata
- Authors
- Brandt, U., & Trumpower, B.
- Venue
- Critical Reviews in Biochemistry and Molecular Biology
- Publisher
- Informa UK Limited
- Published
- 1994-01
- Volume
- 29
- Issue
- 3
- Pages
- 165-197
- ISSN
- 0045-6411 (ISSN-L)
- 1040-9238
- 1549-7798
- OpenAlex
- W2048484224
- Cited by
- 353
- References
- 98
- FWCI
- 1.45
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The Protonmotive Q Cycle in Mitochondria and Bacteria. https://app.cochat.ai/papers/10.3109/10409239409086800
- The paper
- Brandt, U., & Trumpower, B. (1994). The Protonmotive Q Cycle in Mitochondria and Bacteria. Critical Reviews in Biochemistry and Molecular Biology. https://doi.org/10.3109/10409239409086800
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.