ArticleProceedings of the National Academy of Sciences of the United States of America2016
Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Reversible Dimerization of Cytochrome Oxidase in Detergent Solution as Detected by Dynamic Light Scattering.International journal of molecular sciences · 2026Article
- Molecular Biophysics of Class A G Protein Coupled Receptors-Lipids Interactome at a Glance-Highlights from the ABiomolecules · 2023Review
- Monomer and dimer structures of cytochrome boProtein science : a publication of the Protein Society · 2023Article
- Interaction of Terminal Oxidases with Amphipathic Molecules.International journal of molecular sciences · 2023Review
- Structural basis of mammalian complex IV inhibition by steroids.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Assessing the Role of Lipids in the Molecular Mechanism of Membrane Proteins.International journal of molecular sciences · 2021Review
- Article
- CytochromeCells · 2021Review
- The 1.3-Å resolution structure of bovine cytochromeBBA advances · 2021Article
- Review
- The importance of the membrane for biophysical measurements.Nature chemical biology · 2020Review
- Stress-mediated generation of deleterious ROS in healthy individuals - role of cytochrome c oxidase.Journal of molecular medicine (Berlin, Germany) · 2020Review
- Characterizing Thermal Transitions of IgG with Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Monomeric structure of an active form of bovine cytochromeProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo-electron microscopy.Science advances · 2019Article
- Cholesterol Interaction Sites on the Transmembrane Domain of the Hedgehog Signal Transducer and Class F G Protein-Coupled Receptor Smoothened.Structure (London, England : 1993) · 2019Article
- Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry.Science (New York, N.Y.) · 2018Article
- 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
- Lipid binding attenuates channel closure of the outer membrane protein OmpF.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Identifying key membrane protein lipid interactions using mass spectrometry.Nature protocols · 2018Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Bovine cytochrome c oxidase is an integral membrane protein complex comprising 13 protein subunits and associated lipids. Dimerization of the complex has been proposed; however, definitive evidence for the dimer is lacking. We used advanced mass spectrometry methods to investigate the oligomeric state of cytochrome c oxidase and the potential role of lipids and posttranslational modifications in its subunit interfaces. Mass spectrometry of the intact protein complex revealed that both the monomer and the dimer are stabilized by large lipid entities. We identified these lipid species from the purified protein complex, thus implying that they interact specifically with the enzyme. We further identified phosphorylation and acetylation sites of cytochrome c oxidase, located in the peripheral subunits and in the dimer interface, respectively. Comparing our phosphorylation and acetylation sites with those found in previous studies of bovine, mouse, rat, and human cytochrome c oxidase, we found that whereas some acetylation sites within the dimer interface are conserved, suggesting a role for regulation and stabilization of the dimer, phosphorylation sites were less conserved and more transient. Our results therefore provide insights into the locations and interactions of lipids with acetylated residues within the dimer interface of this enzyme, and thereby contribute to a better understanding of its structure in the natural membrane. Moreover dimeric cytochrome c oxidase, comprising 20 transmembrane, six extramembrane subunits, and associated lipids, represents the largest integral membrane protein complex that has been transferred via electrospray intact into the gas phase of a mass spectrometer, representing a significant technological advance.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.