Destabilization of the Quaternary Structure of Bovine Heart Cytochrome c Oxidase upon Removal of Tightly Bound Cardiolipin
Author:
Affiliation:
1. Department of Biochemistry, The University of Texas Health Science Center, San Antonio, Texas 78229-3900, United States
Funder
Welch Foundation
Seventh Framework Programme
National Institute of General Medical Sciences
Vedeck? Grantov? Agent?ra M?VVa? SR a SAV
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00540
Reference35 articles.
1. Evolution of a Regulatory Enzyme: Cytochrome-c Oxidase (Complex IV)
2. The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å
3. Functional binding of cardiolipin to cytochromec oxidase
4. Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase
5. Phospholipase A2 Digestion of Cardiolipin Bound to Bovine Cytochrome c Oxidase Alters Both Activity and Quaternary Structure†
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1. Two mitochondrial DNA polymorphisms modulate cardiolipin binding and lead to synthetic lethality;Nature Communications;2024-01-19
2. Unraveling the mechanisms of cardiolipin function: The role of oxidative polymerization of unsaturated acyl chains;Redox Biology;2023-08
3. Positive cooperativity in the activation of E. coli aquaporin Z by cardiolipin: Potential for lipid-based aquaporin modulators;Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids;2021-05
4. The Interplay among Subunit Composition, Cardiolipin Content, and Aggregation State of Bovine Heart Cytochrome c Oxidase;Cells;2020-12-03
5. Monomeric structure of an active form of bovine cytochrome c oxidase;Proceedings of the National Academy of Sciences;2019-09-18
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