ArticleProceedings of the National Academy of Sciences of the United States of America2011
Crystallographic and online spectral evidence for role of conformational change and conserved water in cytochrome oxidase proton pump.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. 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, 50 citations in OpenAlex.
- Structural and functional mechanisms of cytochrome c oxidase.Journal of inorganic biochemistry · 2025Review
- Structural insights into functional properties of the oxidized form of cytochrome c oxidase.Nature communications · 2023Article
- Accelerated Evolution of CytochromeCells · 2022Article
- Oxidative Stress in Ischemia/Reperfusion Injuries following Acute Ischemic Stroke.Biomedicines · 2022Review
- Role of conformational change and K-path ligands in controlling cytochromeBiochemical Society transactions · 2017Review
- Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature.Scientific reports · 2017Article
- A nanosecond time-resolved XFEL analysis of structural changes associated with CO release from cytochrome c oxidase.Science advances · 2017Article
- Water exit pathways and proton pumping mechanism in B-type cytochrome c oxidase from molecular dynamics simulations.Biochimica et biophysica acta · 2016Article
- Biomimetic Membranes for Multi-Redox Center Proteins.International journal of molecular sciences · 2016Review
- Structural Changes and Proton Transfer in Cytochrome c Oxidase.Scientific reports · 2015Article
- Linking chemical electron-proton transfer to proton pumping in cytochrome c oxidase: broken-symmetry DFT exploration of intermediates along the catalytic reaction pathway of the iron-copper dinuclear complex.Inorganic chemistry · 2014Article
- Time-resolved surface-enhanced IR-absorption spectroscopy of direct electron transfer to cytochrome c oxidase from R. sphaeroides.Biophysical journal · 2013Article
- Single mutations that redirect internal proton transfer in the ba3 oxidase from Thermus thermophilus.Biochemistry · 2013Article
- Role of aspartate 132 at the orifice of a proton pathway in cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A conserved amphipathic ligand binding region influences k-path-dependent activity of cytochrome C oxidase.Biochemistry · 2013Article
- Cellular and molecular mechanisms of mitochondrial function.Best practice & research. Clinical endocrinology & metabolism · 2012Review
- From static structure to living protein: computational analysis of cytochrome c oxidase main-chain flexibility.Biophysical journal · 2012Article
- Gating and regulation of the cytochrome c oxidase proton pump.Biochimica et biophysica acta · 2012Review
- Design of photoactive ruthenium complexes to study electron transfer and proton pumping in cytochrome oxidase.Biochimica et biophysica acta · 2012Review
- Reconstitution of respiratory oxidases in membrane nanodiscs for investigation of proton-coupled electron transfer.FEBS letters · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Crystal structures in both oxidized and reduced forms are reported for two bacterial cytochrome c oxidase mutants that define the D and K proton paths, showing conformational change in response to reduction and the loss of strategic waters that can account for inhibition of proton transfer. In the oxidized state both mutants of the Rhodobacter sphaeroides enzyme, D132A and K362M, show overall structures similar to wild type, indicating no long-range effects of mutation. In the reduced state, the mutants show an altered conformation similar to that seen in reduced wild type, confirming this reproducible, reversible response to reduction. In the strongly inhibited D132A mutant, positions of residues and waters in the D pathway are unaffected except in the entry region close to the mutation, where a chloride ion replaces the missing carboxyl and a 2-Å shift in N207 results in loss of its associated water. In K362M, the methionine occupies the same position as the original lysine, but K362- and T359-associated waters in the wild-type structure are missing, likely accounting for the severe inhibition. Spectra of oxidized frozen crystals taken during X-ray radiation show metal center reduction, but indicate development of a strained configuration that only relaxes to a native form upon annealing. Resistance of the frozen crystal to structural change clarifies why the oxidized conformation is observable and supports the conclusion that the reduced conformation has functional significance. A mechanism is described that explains the conformational change and the incomplete response of the D-path mutant.
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