Mitochondrial Electron Transport and Oxidative Phosphorylation
Abstract
The electron transport chain is made up of several integral membrane complexes that were fractionated almost three decades ago: NADH-ubiquinone oxidoreductase (complex I), ubiquinone-cytochrome-c oxidoreductase (complex III), and cytochrome c oxidase (complex IV). Succinate-ubiquinone oxidoreductase (Complex II) connects the Krebs cycle directly to the electron transport chain. Ubiquinone and cytochrome c are considered mobile carriers, with Q/QH2 mobile in the inner membrane and cytochrome c soluble and diffusible in the intermembrane space. High-resolution crystal structures for all but complex I are available. The direction of the flow of electrons is now well understood, both between complexes and within complexes, but the precise mechanism of the proton pumping that accompanies electron transport through complexes I, III, and IV remains a challenge for the future. The chemiosmotic hypothesis has emerged triumphant, providing a theoretical framework for phenomena such as coupling, acceptor control by ADP, and thermogenesis. Its generalization to include photorespiration in chloroplasts and oxidative phophorylation in bacteria is universally accepted. The elucidation of the structure and mechanism of the ATP synthase as the smallest molecular rotary engine driven by a proton flux is a crowning achievement after a century of research in bioenergetics. Although proton pumping is a central event in electron transport and oxidative phosphorylation, it is becoming increasingly clear that transport(s) of other ions in and out of the matrix are very active processes, and mitochondria play a key role in the control of intracellular/cytosolic calcium levels.
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Calcium, reactive oxygen species, high pH, low membrane potential, and oxidized pyridine nucleotides may lead to opening of the mitochondrial permeability transition pore.
“Calcium, ROS, high pH, low membrane potential, and oxidized pyridine nucleotides all may lead to opening of the mitochondrial permeability transition pore (MPTP) (284).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [284]
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- Authors
- Scheffler, I. E.
- Affiliations
- University of California San Diego (US)
- Corresponding author
- Immo E. Scheffler
- Venue
- Mitochondria
- Publisher
- Wiley
- Published
- 1999-06-21
- Pages
- 141-245
- OpenAlex
- W1504444610
- Cited by
- 21
- References
- 1
- Citations by year
- 2022: 1 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 1 · 2015: 1 · 2012: 1
- Type
- other
- Language
- en
- Open access
- closed
- 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
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- mitochondrial electron transport chain, oxidative phosphorylation, complex I, cytochrome bc1 complex, cytochrome c oxidase, complex II, coenzyme Q10, cytochrome c, chemiosmotic theory, proton translocation, ATP synthase, photorespiration, thermogenesis, ion transport, intracellular calcium homeostasis, bioenergetics
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