ArticleProceedings of the National Academy of Sciences of the United States of America2015
Mutation of a single residue in the ba3 oxidase specifically impairs protonation of the pump site.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochromeScience advances · 2023Article
- A simple goniometer-compatible flow cell for serial synchrotron X-ray crystallography.Journal of applied crystallography · 2023Article
- Probing the Proton-Loading Site of CytochromeMolecules (Basel, Switzerland) · 2020Article
- Oxygen Activation and Energy Conservation by Cytochrome c Oxidase.Chemical reviews · 2018Review
- A Water Dimer Shift Activates a Proton Pumping Pathway in the PInorganic chemistry · 2018Article
- Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature.Scientific reports · 2017Article
- Isolation of yeast complex IV in native lipid nanodiscs.Biochimica et biophysica acta · 2016Article
- ns-μs Time-Resolved Step-Scan FTIR of ba₃ Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927.International journal of molecular sciences · 2016Article
- Rapid Electron Transfer within the III-IV Supercomplex in Corynebacterium glutamicum.Scientific reports · 2016Article
- Water exit pathways and proton pumping mechanism in B-type cytochrome c oxidase from molecular dynamics simulations.Biochimica et biophysica acta · 2016Article
- A broken-symmetry density functional study of structures, energies, and protonation states along the catalytic O-O bond cleavage pathway in ba3 cytochrome c oxidase from Thermus thermophilus.Physical chemistry chemical physics : PCCP · 2016Article
- Regulatory role of the respiratory supercomplex factors in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Analyzing the electrogenicity of cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The ba3-type cytochrome c oxidase from Thermus thermophilus is a membrane-bound protein complex that couples electron transfer to O2 to proton translocation across the membrane. To elucidate the mechanism of the redox-driven proton pumping, we investigated the kinetics of electron and proton transfer in a structural variant of the ba3 oxidase where a putative "pump site" was modified by replacement of Asp372 by Ile. In this structural variant, proton pumping was uncoupled from internal electron transfer and O2 reduction. The results from our studies show that proton uptake to the pump site (time constant ∼65 μs in the wild-type cytochrome c oxidase) was impaired in the Asp372Ile variant. Furthermore, a reaction step that in the wild-type cytochrome c oxidase is linked to simultaneous proton uptake and release with a time constant of ∼1.2 ms was slowed to ∼8.4 ms, and in Asp372Ile was only associated with proton uptake to the catalytic site. These data identify reaction steps that are associated with protonation and deprotonation of the pump site, and point to the area around Asp372 as the location of this site in the ba3 cytochrome c oxidase.
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