Cited by 51Enzyme Structure and FunctionMitochondrial Function and PathologyMetal-Catalyzed Oxygenation Mechanisms

Escherichia coli succinate dehydrogenase variant lacking the heme b

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Tran, Quang M., Rothery, Richard A., Maklashina, Elena, Cecchini, Gary, Weiner, Joel H.·2007·Proceedings of the National Academy of Sciences

Abstract

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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Crossref · 10.1073/pnas.0707732104

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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
Published
2007-11-13
Volume
104
Issue
46
Pages
18007-18012
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
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
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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