The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
The efficiency and plasticity of mitochondrial energy transduction.
Abstract
Since it was first realized that biological energy transduction involves oxygen and ATP, opinions about the amount of ATP made per oxygen consumed have continually evolved. The coupling efficiency is crucial because it constrains mechanistic models of the electron-transport chain and ATP synthase, and underpins the physiology and ecology of how organisms prosper in a thermodynamically hostile environment. Mechanistically, we have a good model of proton pumping by complex III of the electron-transport chain and a reasonable understanding of complex IV and the ATP synthase, but remain ignorant about complex I. Energy transduction is plastic: coupling efficiency can vary. Whether this occurs physiologically by molecular slipping in the proton pumps remains controversial. However, the membrane clearly leaks protons, decreasing the energy funnelled into ATP synthesis. Up to 20% of the basal metabolic rate may be used to drive this basal leak. In addition, UCP1 (uncoupling protein 1) is used in specialized tissues to uncouple oxidative phosphorylation, causing adaptive thermogenesis. Other UCPs can also uncouple, but are tightly regulated; they may function to decrease coupling efficiency and so attenuate mitochondrial radical production. UCPs may also integrate inputs from different fuels in pancreatic beta-cells and modulate insulin secretion. They are exciting potential targets for treatment of obesity, cachexia, aging and diabetes.
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“Thus, the activation of UCP2 protects the -cell from the deleterious effects of excess ROS (257) by dissipating the proton gradient and decreasing ROS production in a controlled negative feedback manner (Fig. 4).”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [257]
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Cites
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Topology of superoxide production from different sites in the mitochondrial electron transport chain
St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545
Self-citationSuperoxide activates mitochondrial uncoupling proteins
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Self-citationMolecular Architecture of the Rotary Motor in ATP Synthase
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Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins
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Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3
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Self-citationThe mitochondrial uncoupling-protein homologues
Krauss, S., Zhang, C., & Lowell, B. B. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1592 · Cited by 670
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Research works printed but not linked: 3
- Brand, 1994, Biochemist, 16, 20
- Ainscow, 1995, BioThermoKinetics in the Post Genomic Era, 192
- Porter, 1995, Am. J. Physiol., 269, R1213
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Assessing mitochondrial dysfunction in cells
Brand, M. D., & Nicholls, D. G. (2011) · Biochemical Journal · doi:10.1042/bj20110162 · Cited by 2,436
Self-citationMolecular Aspects of Thyroid Hormone Actions
Cheng, S.-Y., Leonard, J. L., & Davis, P. J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0007 · Cited by 1,384
The assembly, regulation and function of the mitochondrial respiratory chain
Vercellino, I., & Sazanov, L. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00415-0 · Cited by 1,015
Wu, M., Neilson, A., Swift, A. L., Moran, R., Tamagnine, J., Parslow, D., Armistead, S., Lemire, K., Orrell, J., Teich, J., et al. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00247.2006 · Cited by 927
Mitochondria are required for pro-ageing features of the senescent phenotype
Correia‐Melo, C., Marques, F. D., Anderson, R., Hewitt, G., Hewitt, R., Cole, J., Carroll, B. M., Miwa, S., Birch, J., Merz, A., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201592862 · Cited by 796
Metadata
- Authors
- Brand, M. D.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- Corresponding author
- Brand, M.D.
- ORCID
- Brand, M.D.
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2005-10-26
- Volume
- 33
- Issue
- 5
- Pages
- 897-904
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W2021952329
- Cited by
- 406
- References
- 57
- Citations by year
- 2026: 12 · 2025: 17 · 2024: 8 · 2023: 25 · 2022: 17 · 2021: 19 · 2020: 22 · 2019: 20 · 2018: 19 · 2017: 30 · 2016: 21 · 2015: 23 · 2014: 27 · 2013: 12 · 2012: 27
- FWCI
- 0.91
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- mitochondrial energy transduction, coupling efficiency, electron transport chain, complex I, ATP synthase, proton leak, UCP1, thermogenesis, mitochondrial uncoupling, mitochondrial reactive oxygen species, beta-cell insulin secretion, obesity, cachexia, aging, diabetes mellitus
- MeSH terms
- Adenosine Triphosphate, Animals, Energy Metabolism, Mitochondria, Models, Biological, Oxygen Consumption, Uncoupling Agents
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