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Structure and Mechanism of Respiratory III-IV Supercomplexes in Bioenergetic Membranes
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0003-3860-4988
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0002-3328-763X
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0003-0853-6785
Number of Authors: 32021 (English)In: Chemical Reviews, ISSN 0009-2665, E-ISSN 1520-6890, Vol. 121, no 15, p. 9644-9673Article, review/survey (Refereed) Published
Abstract [en]

In the final steps of energy conservation in aerobic organisms, free energy from electron transfer through the respiratory chain is transduced into a proton electrochemical gradient across a membrane. In mitochondria and many bacteria, reduction of the dioxygen electron acceptor is catalyzed by cytochrome c oxidase (complex IV), which receives electrons from cytochrome bc(1) (complex III), via membrane-bound or watersoluble cytochrome c. These complexes function independently, but in many organisms they associate to form supercomplexes. Here, we review the structural features and the functional significance of the nonobligate III2IV1/2 Saccharomyces cerevisiae mitochondrial super-complex as well as the obligate III2IV2 supercomplex from actinobacteria. The analysis is centered around the Q-cycle of complex III, proton uptake by CytcO, as well as mechanistic and structural solutions to the electronic link between complexes III and IV.

Place, publisher, year, edition, pages
2021. Vol. 121, no 15, p. 9644-9673
National Category
Chemical Sciences
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URN: urn:nbn:se:su:diva-197423DOI: 10.1021/acs.chemrev.1c00140ISI: 000685239600009PubMedID: 34184881OAI: oai:DiVA.org:su-197423DiVA, id: diva2:1599982
Available from: 2021-10-03 Created: 2021-10-03 Last updated: 2022-03-23Bibliographically approved

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Brzezinski, PeterMoe, AgnesÄdelroth, Pia

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