Rich, PR;
(2021)
Bioenergetics Theory and Components | Chemiosmotic Theory☆.
In:
Encyclopedia of Biological Chemistry.
(pp. 7-14).
Elsevier
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Text
Rich_Article version 14 Jan 2020 HARVARD style.pdf Access restricted to UCL open access staff Download (325kB) |
Abstract
The majority of cellular ATP synthesis is usually associated with respiratory and photosynthetic processes that are catalyzed by complex redox and ATP synthase enzymes embedded in ion-impermeable lipid membranes. The redox reactions are coupled indirectly to ATP synthesis through an electrochemical gradient of protons, the protonmotive force, which is formed across the membrane in which they are embedded. The protonmotive force powers the energy-requiring synthesis of ATP and can also power active transport of metabolites across membranes. This “chemiosmotic hypothesis” of the mechanism of such coupling was first postulated by Peter Mitchell in 1961 and is now widely accepted as the chemiosmotic theory.
Type: | Book chapter |
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Title: | Bioenergetics Theory and Components | Chemiosmotic Theory☆ |
ISBN-13: | 9780128194607 |
DOI: | 10.1016/B978-0-12-809633-8.21387-3 |
Publisher version: | https://doi.org/10.1016/B978-0-12-809633-8.21387-3 |
Language: | English |
Additional information: | This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions. |
Keywords: | ATP synthesis, Electron transfer, Energy coupling, Membrane transport, Mitochondria, Peter Mitchell, Photosynthesis, Proton gradient, Protonmotive force, Quinones, Redox loop, Respiration |
UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology |
URI: | https://discovery.ucl.ac.uk/id/eprint/10137617 |
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