ArticleBiochemistry2013
A conserved amphipathic ligand binding region influences k-path-dependent activity of cytochrome C oxidase.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Electron transfer between complexes III and IV in S. cerevisiae mitochondrial membranes.FEBS letters · 2026Article
- Structural basis of Neisseria meningitidis quinol dependent nitric oxide reductase activation by dimerization.Communications biology · 2026Article
- A Novel Link Between Electron Transport Chain Modulation and mcl-PHA Production in Pseudomonas aeruginosa 5300 Using Azide as a Modulator.Environmental microbiology reports · 2026Article
- Sulphide and oleic acid synergism in accelerating mcl-PHA biopolymer production inBiochemistry and biophysics reports · 2025Article
- Cholesterol Attenuates the Pore-Forming Capacity of CARC-Containing Amphipathic Peptides.International journal of molecular sciences · 2025Article
- Interaction of Terminal Oxidases with Amphipathic Molecules.International journal of molecular sciences · 2023Review
- Interaction of Amphipathic Peptide from Influenza Virus M1 Protein with Mitochondrial Cytochrome Oxidase.International journal of molecular sciences · 2023Article
- Cryo-EM structure and function of S. pombe complex IV with bound respiratory supercomplex factor.Communications chemistry · 2023Article
- Structural basis of mammalian complex IV inhibition by steroids.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Direct Interaction of Mitochondrial CytochromeCells · 2022Article
- Complex Interplay of Heme-Copper Oxidases with Nitrite and Nitric Oxide.International journal of molecular sciences · 2022Review
- Article
- Monomeric structure of an active form of bovine cytochromeProceedings of the National Academy of Sciences of the United States of America · 2019Article
- The K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain.Biochimica et biophysica acta. Bioenergetics · 2018Article
- Role of conformational change and K-path ligands in controlling cytochromeBiochemical Society transactions · 2017Review
- Translocator Protein 18 kDa (TSPO): An Old Protein with New Functions?Biochemistry · 2016Article
- Article
- Article
- Computational prediction and in vitro analysis of potential physiological ligands of the bile acid binding site in cytochrome c oxidase.Biochemistry · 2013Article
- Functions of the hydrophilic channels in protonmotive cytochrome c oxidase.Journal of the Royal Society, Interface · 2013Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A conserved, crystallographically defined bile acid binding site was originally identified in the membrane domain of mammalian and bacterial cytochrome c oxidase (CcO). Current studies show other amphipathic molecules including detergents, fatty acids, steroids, and porphyrins bind to this site and affect the already 50% inhibited activity of the E101A mutant of Rhodobacter sphaeroides CcO as well as altering the activity of wild-type and bovine enzymes. Dodecyl maltoside, Triton X100, C12E8, lysophophatidylcholine, and CHOBIMALT detergents further inhibit RsCcO E101A, with lesser inhibition observed in wild-type. The detergent inhibition is overcome in the presence of micromolar concentrations of steroids and porphyrin analogues including deoxycholate, cholesteryl hemisuccinate, bilirubin, and protoporphyrin IX. In addition to alleviating detergent inhibition, amphipathic carboxylates including arachidonic, docosahexanoic, and phytanic acids stimulate the activity of E101A to wild-type levels by providing the missing carboxyl group. Computational modeling of dodecyl maltoside, bilirubin, and protoporphyrin IX into the conserved steroid site shows energetically favorable binding modes for these ligands and suggests that a groove at the interface of subunit I and II, including the entrance to the K-path and helix VIII of subunit I, mediates the observed competitive ligand interactions involving two overlapping sites. Spectral analysis indicates that ligand binding to this region affects CcO activity by altering the K-path-dependent electron transfer equilibrium between heme a and heme a(3). The high affinity and specificity of a number of compounds for this region, and its conservation and impact on CcO activity, support its physiological significance.
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