ArticleBiochimica et biophysica acta. Bioenergetics2018
The K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain.
Article in Biochimica et biophysica acta. Bioenergetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- The flexible chain: regulation of structure and activity of ETC complexes defines rate of ATP synthesis and sites of superoxide generation.Biophysical reviews · 2025Review
- Structural and functional mechanisms of cytochrome c oxidase.Journal of inorganic biochemistry · 2025Review
- Interaction of Terminal Oxidases with Amphipathic Molecules.International journal of molecular sciences · 2023Review
- Interplay of Hydration and Protonation Dynamics in the K-Channel of Cytochrome c Oxidase.Biomolecules · 2022Article
- 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
- Article
- Monomeric structure of an active form of bovine cytochromeProceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Three mutant forms of Rhodobacter sphaeroides cytochrome c oxidase (RsCcO) were created to test for multiple K-path entry sites (E101W), the existence of an "upper ligand site" (M350 W), and the nature and binding specificity of the "lower ligand site" (P315W/E101A) in the region of a crystallographically-defined deoxycholate at the K-path entrance. The effects of inhibitory and stimulatory detergents (dodecyl maltoside and Tween20) on these mutants are presented, as well as competition with other ligands, including the potentially physiologically relevant ligands cholesterol and retinoic acid. Ligands are shown to be able to compete with natural lipids to affect the activity of membrane-bound RsCcO. Results point to a single K-path entrance site at E101, with a single ligand binding pocket proximal to the entrance. The affinity of this pocket for amphipathic ligands is enhanced by removal of the E101 carboxyl and blocked by substituting a tryptophan in this area. A new crystal structure of the E101A mutant of RsCcO is presented that illustrates the structural basis of these results, showing that the loss of the E101 carboxyl creates a more hydrophobic groove consistent with altered ligand affinities.
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