The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Cardiolipin: a proton trap for oxidative phosphorylation
Abstract
The role of specific lipid structures in biological membranes has been elusive. There are hundreds of them in nature. Why has nature made them? How do they aid in the functioning of membrane proteins? Genetics with its ‘knock out’ organisms declares that functions persist in the absence of any particular lipid. Nonetheless some lipids, such as cardiolipin (CL), are associated with particular functions in the cell. It may merely expand the variety of culture conditions (pH, temperature, etc.) under which the wild‐type organism survives. This article explores a unique role of CL as a proton trap within membranes that conduct oxidative phosphorylation and therefore the synthesis of ATP. CL's pK 2 (above 8.0) provides a role for it as a headgroup proton trap for oxidative phosphorylation. It suggests why CL is found in membranes that pump protons. The high pK 2 also indicates that the headgroup has but one negative charge in the neutral pH range. Data on the binding of CL to all of the oxidative phosphorylation proteins suggest that the CL may aggregate the oxidative phosphorylation proteins into a patch while it restricts pumped protons within its headgroup domain – supplying protons to the ATP synthase with minimal changes in the bulk phase pH.
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
Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
Schägger, H., & Pfeiffer, K. (2000) · The EMBO Journal · doi:10.1093/emboj/19.8.1777 · Cited by 1,356
The biosynthesis and functional role of cardiolipin
Schlame, M., Rua, D., & Greenberg, M. L. (2000) · Progress in Lipid Research · doi:10.1016/s0163-7827(00)00005-9 · Cited by 810
Handbook of Lipid Bilayers, Second Edition
Marsh, D. (1990) · Cited by 514
CYTOCHROME C OXIDASE: Structure and Spectroscopy
Michel, H., Behr, J., Harrenga, A., & Kannt, A. (1998) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.27.1.329 · Cited by 450
Mileykovskaya, E., & Dowhan, W. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.4.1172-1175.2000 · Cited by 432
Jiang, F., Ryan, M. T., Schlame, M., Zhao, M., Gu, Z., Klingenberg, M., Pfanner, N., & Greenberg, M. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909868199 · Cited by 413
Proton migration along the membrane surface and retarded surface to bulk transfer
Heberle, J., Riesle, J., Thiedemann, G., Oesterhelt, D., & Dencher, N. A. (1994) · Nature · doi:10.1038/370379a0 · Cited by 358
Self-citationCrystal structure of the yeast cytochrome bc 1 complex with its bound substrate cytochrome c
Lange, C., & Hunte, C. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052704699 · Cited by 343
PETIT, J., MAFTAH, A., RATINAUD, M., & JULIEN, R. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17285.x · Cited by 334
The rotary mechanism of ATP synthase
Stock, D., Gibbons, C., Arechaga, I., Leslie, A. G., & Walker, J. E. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00147-0 · Cited by 322
Cited by
Antimicrobial Peptides Targeting Gram-Positive Bacteria
Malanovic, N., & Lohner, K. (2016) · Pharmaceuticals · doi:10.3390/ph9030059 · Cited by 420
Microbial diversity and biogeochemical cycling in soda lakes
Sorokin, D. Y., Berben, T., Melton, E. D., Overmars, L., Vavourakis, C. D., & Muyzer, G. (2014) · Extremophiles · doi:10.1007/s00792-014-0670-9 · Cited by 344
Kagan, V. E., Borisenko, G. G., Tyurina, Y. Y., Tyurin, V. A., Jiang, J., Potapovich, A. I., Kini, V., Amoscato, A. A., & Fujii, Y. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.08.016 · Cited by 342
Kiebish, M. A., Han, X., Cheng, H., Chuang, J. H., & Seyfried, T. N. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800319-jlr200 · Cited by 293
Lipid domains in bacterial membranes
Matsumoto, K., Kusaka, J., Nishibori, A., & Hara, H. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05317.x · Cited by 289
Metadata
- Authors
- Haines, T. H., & Dencher, N. A.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2002-08-29
- Volume
- 528
- Issue
- 1-3
- Pages
- 35-39
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2031227547
- Cited by
- 405
- References
- 33
- FWCI
- 3.02
- 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: Cardiolipin: a proton trap for oxidative phosphorylation. https://app.cochat.ai/papers/10.1016/s0014-5793(02)03292-1
- The paper
- Haines, T. H., & Dencher, N. A. (2002). Cardiolipin: a proton trap for oxidative phosphorylation. FEBS Letters. https://doi.org/10.1016/s0014-5793(02)03292-1
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.
