Escherichia coli succinate dehydrogenase variant lacking the heme b
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The Escherichia coli enzyme succinate:ubiquinone oxidoreductase [(succinate dehydrogenase (SdhCDAB)] couples succinate oxidation to ubiquinone reduction and is structurally and functionally equivalent to mitochondrial complex II, an essential component of the aerobic respiratory chain and tricarboxylic acid cycle. All such enzymes contain a heme within their membrane anchor domain with a highly contentious, but as-yet-undetermined, function. Here, we report the generation of a complex II that lacks heme, which is confirmed by both optical and EPR spectroscopy. Despite the absence of heme, this mutant still assembles properly and retains physiological activity. However, the mutants lacking heme are highly sensitive to the presence of detergent. In addition, the heme does not appear to be involved in reactive oxygen species suppression. Our results indicate that redox cycling of the heme in complex II is not essential for the enzyme's ubiquinol reductase activity.
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Mutants of E. coli SQR lacking heme b showed unchanged ROS generation, indicating that heme b does not serve as a sink for excess electrons.
“Mutants of E. coli SQR that do not contain heme b showed an unchanged ROS generation, indicating that this prosthetic group is not serving as a 'sink' for excess electrons [102,103].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [102]
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Succinate Dehydrogenase (Complex II)
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- Authors
- Tran, Q. M., Rothery, R. A., Maklashina, E., Cecchini, G., & Weiner, J. H.
- Affiliations
- University of Alberta (CA)
- San Francisco VA Medical Center (US)
- *Department of Biochemistry, Membrane Protein Research Group, University of Alberta, Edmonton, AB, Canada T6G 2H7;
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2007-11-13
- Volume
- 104
- Issue
- 46
- Pages
- 18007-18012
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2084287
- OpenAlex
- W2000016159
- Cited by
- 51
- References
- 31
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 3 · 2019: 2 · 2018: 4 · 2017: 2 · 2016: 1 · 2015: 2 · 2014: 1 · 2013: 4 · 2012: 9
- FWCI
- 2.58
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs
- Fondation pour la Recherche Médicale
- National Institutes of Health
- Canadian Institutes of Health Research
- National Institute of General Medical Sciences (R01GM061606)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- succinate dehydrogenase, complex II, heme b, Escherichia coli, enzyme assembly, detergent sensitivity, reactive oxygen species, redox cycling, aerobic respiratory chain, TCA cycle
- MeSH terms
- Detergents, Electron Spin Resonance Spectroscopy, Escherichia coli, Heme, Potentiometry, Spectrophotometry, Ultraviolet, Succinate Dehydrogenase, Mutagenesis, Site-Directed
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