The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane.
Open accessAbstract
The amino acid sequences of cytochrome b of complex III from five different mitochondrial sources (human, bovine, mouse, yeast, and Aspergillus nidulans) and the chloroplast cytochrome b6 from spinach show a high degree of homology. Calculation of the distribution of hydrophobic residues with a "hydropathy" function that is conserved in this family of proteins implies that the membrane-folding pattern of the 42-kilodalton (kDa) mitochondrial cytochromes involves 8-9 membrane-spanning domains. The smaller 23-kDa chloroplast cytochrome appears to fold in five spanning domains that are similar to the first five of the mitochondria. Four highly conserved histidines are considered to be the likely ligands for the two hemes. The positions of the histidines along the spanning segments and in a cross section of the membrane-spanning alpha helices implies that two ligand pairs, His-82-His-197/198 and His-96-His-183, bridge the spanning peptides II and V, and the two hemes reside on opposite sides of the hydrophobic membrane core. In addition, the 17-kDa protein of the chloroplast b6-f complex appears to contain one or more of the functions of the COOH-terminal end of the mitochondrial cytochrome b polypeptide.
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Anderson, S., de Bruijn, M. H. L., Coulson, A. R., Eperon, I. C., Sanger, F., & Young, I. G. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90137-1 · Cited by 1,472
Cited by
Sumimoto, H. (2008) · The FEBS Journal · doi:10.1111/j.1742-4658.2008.06488.x · Cited by 721
The Protonmotive Q Cycle in Mitochondria and Bacteria
Brandt, U., & Trumpower, B. (1994) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239409086800 · Cited by 353
Hypothesis about the function of membrane-buried proline residues in transport proteins.
Brandl, C. J., & Deber, C. M. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.4.917 · Cited by 337
Huang, L.-S., Cobessi, D., Tung, E. Y., & Berry, E. A. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.05.053 · Cited by 304
Finegold, A. A., Shatwell, K. P., Segal, A. W., Klausner, R. D., & Dancis, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31021 · Cited by 213
Metadata
- Authors
- Widger, W. R., Cramer, W. A., Herrmann, R. G., & Trebst, A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1984-02
- Volume
- 81
- Issue
- 3
- Pages
- 674-678
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2020520553
- Cited by
- 401
- References
- 1
- FWCI
- 15.21
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane. https://app.cochat.ai/papers/10.1073/pnas.81.3.674
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- Widger, W. R., Cramer, W. A., Herrmann, R. G., & Trebst, A. (1984). Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.81.3.674
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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