Progress in understanding structure-function relationships in respiratory chain complex II.
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Complex II (succinate:quinone oxidoreductase) of aerobic respiratory chains oxidizes succinate to fumarate and passes the electrons directly into the quinone pool. It serves as the only direct link between activity in the citric acid cycle and electron transport in the membrane. Finer details of these reactions and interactions are but poorly understood. However, complex II has extremely similar structural and catalytic properties to quinol:fumarate oxidoreductases of anaerobic organisms, for which X‐ray structures have recently become available. These offer new insights into structure–function relationships of this class of flavoenzymes, including evidence favoring protein movement during catalysis.
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SDH is both a Krebs cycle component that oxidizes succinate to fumarate and a mitochondrial respiratory chain component that transfers electrons to the ubiquinone pool.
“This enzyme is both a component of the Krebs cycle, by oxidizing succinate to fumarate, and of the mitochondrial respiratory chain, by transferring electrons to the ubiquinone pool [8].”
From A HIF1α Regulatory Loop Links Hypoxia and Mitochondrial Signals in Pheochromocytomas (2005) · cites this paper as [8]
Mutations in SdhB, SdhC, or SdhD are linked to tumorigenesis in the form of autosomal-dominant familial paragangliomas and pheochromocytomas.
“However, mutations in subunit SdhB, SdhC, or SdhD are linked to tumorigenesis in the form of autosome-dominant familial paragangliomas and pheochromocytomas (1, 3, 16, 19, 33).”
Complex II oxidizes succinate to fumarate and transfers electrons to ubiquinone through a sequence involving flavin in SdhA, iron-sulfur clusters in SdhB, heme in SdhC, and the ubiquinone binding site in SdhC and SdhD.
“Complex II oxidizes succinate to fumarate and transfers the electrons to ubiquinone through a sequence of steps involving a flavin moiety in SdhA, a set of iron-sulfur clusters in SdhB, a heme group in SdhC, and the ubiquinone binding site in SdhC and SdhD (Fig. 1) (1, 9).”
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References 44 · Cited by 144
Research works printed but not linked: 6
- Ackrell, B.A.C., Johnson, M.K., Gunsalus, R.P. and Cecchini, G. (1992) in: Chemistry and Biochemistry of Flavoproteins (Mu « ller, F., Ed.), Vol. III, pp. 229^297, CRC Press, Boca Raton, FL.
- Vik, S.B. and Hate¢, Y. (1981) Proc. Natl. Acad. Sci. USA 78, 6749^6753.
- Salerno, J.C. (1991) Biochem. Soc. Trans. 19, 599^605.
- Dutton, P.L., Chen, X., Page, C.C., Huang, T., Ohnishi, T. and Moser, C.C. (1998) in: Biological Electron Transfer Chains: Ge- netics, Composition and Mode of Operation (Canters, G.W. and Vijgenboom, E., Eds.) pp. 3^8, Kluwer Academic, Dordrecht.
- Allen, J.P., Feher, G., Yeates, T.O., Komiya, H. and Rees, D.C. (1988) Proc. Natl. Acad. Sci. USA 85, 8487^8491.
- Ruzicka, F.J., Beinert, H., Schepler, K.L., Dunham, W.R. and Sands, R.H. (1975) Proc. Natl. Acad. Sci. USA 72, 2886^2890.
- Authors
- Ackrell, B. A. C.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Ackrell, Brian A.C
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2000-01-18
- Volume
- 466
- Issue
- 1
- Pages
- 1-5
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1972889641
- Cited by
- 144
- References
- 44
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 3 · 2023: 6 · 2022: 4 · 2021: 5 · 2020: 3 · 2019: 3 · 2018: 4 · 2017: 5 · 2016: 4 · 2015: 2 · 2014: 6 · 2013: 3 · 2012: 5
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service
- National Heart, Lung, and Blood Institute (HL-16521)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- respiratory chain complex II, structure-function relationship, flavoenzyme, electron transport, succinate oxidation, fumarate, quinone pool
- MeSH terms
- Catalysis, Electron Transport, Escherichia coli, Iron-Sulfur Proteins, Models, Molecular, Multienzyme Complexes, Oxidoreductases, Protein Conformation, Succinate Dehydrogenase, Wolinella, Protein Structure, Secondary, Protein Structure, Quaternary, Electron Transport Complex II
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