Out of plane distortions of the heme b of Escherichia coli succinate dehydrogenase
Open accessAbstract
The role of the heme b in Escherichia coli succinate dehydrogenase is highly ambiguous and its role in catalysis is questionable. To examine whether heme reduction is an essential step of the catalytic mechanism, we generated a series of site-directed mutations around the heme binding pocket, creating a library of variants with a stepwise decrease in the midpoint potential of the heme from the wild-type value of +20 mV down to -80 mV. This difference in midpoint potential is enough to alter the reactivity of the heme towards succinate and thus its redox state under turnover conditions. Our results show both the steady state succinate oxidase and fumarate reductase catalytic activity of the enzyme are not a function of the redox potential of the heme. As well, lower heme potential did not cause an increase in the rate of superoxide production both in vitro and in vivo. The electron paramagnetic resonance (EPR) spectrum of the heme in the wild-type enzyme is a combination of two distinct signals. We link EPR spectra to structure, showing that one of the signals likely arises from an out-of-plane distortion of the heme, a saddled conformation, while the second signal originates from a more planar orientation of the porphyrin ring.
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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 [103]
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- Authors
- Tran, Q. M., Fong, C., Rothery, R. A., Maklashina, E., Cecchini, G., & Weiner, J. H.
- Affiliations
- University of Alberta (CA)
- San Francisco VA Medical Center (US)
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-02-29
- Volume
- 7
- Issue
- 2
- Pages
- e32641
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3290573
- OpenAlex
- W2008446632
- Cited by
- 12
- References
- 39
- Citations by year
- 2022: 1 · 2020: 1 · 2018: 2 · 2017: 1 · 2015: 1 · 2014: 1 · 2013: 3 · 2012: 2
- FWCI
- 1.22
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, public-domain)
- Europe PMC (PubMed Central) (publishedVersion, public-domain)
- PubMed Central (publishedVersion, public-domain)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- U.S. Department of Veterans Affairs (I01 BX001077)
- Office of Research and Development
- National Institutes of Health
- Canadian Institutes of Health Research (MOP89735)
- National Institute of General Medical Sciences (GM61606, R01GM061606)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Keywords
- heme b, succinate dehydrogenase, Escherichia coli, heme redox potential, heme reduction, superoxide production, EPR spectra
- MeSH terms
- Catalysis, Cell Membrane, Electron Spin Resonance Spectroscopy, Escherichia coli, Heme, Humans, Molecular Conformation, Mutation, Oxidation-Reduction, Porphyrins, Spectrophotometry, Ultraviolet, Succinate Dehydrogenase, Mutagenesis, Site-Directed, Reactive Oxygen Species
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