ArticleProceedings of the National Academy of Sciences of the United States of America2006
Controlled uncoupling and recoupling of proton pumping in cytochrome c oxidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 69 citations in OpenAlex.
- Membrane-domain mutations in respiratory complex I impede catalysis but do not uncouple proton pumping from ubiquinone reduction.PNAS nexus · 2022Article
- Electric fields control water-gated proton transfer in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structure and Mechanism of Respiratory III-IV Supercomplexes in Bioenergetic Membranes.Chemical reviews · 2021Review
- AspThe Journal of biological chemistry · 2020Article
- A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mechanism of proton transfer through the KBiochimica et biophysica acta. Bioenergetics · 2018Article
- Hydrogen-Bonded Network and Water Dynamics in the D-channel of Cytochrome c Oxidase.The Journal of membrane biology · 2018Article
- pKProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Analyzing the electrogenicity of cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structural Changes and Proton Transfer in Cytochrome c Oxidase.Scientific reports · 2015Article
- Microscopic basis for kinetic gating in Cytochrome c oxidase: insights from QM/MM analysis.Chemical science · 2015Article
- 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
- Role of the -PEWY-glutamate in catalysis at the Q(o)-site of the Cyt bc(1) complex.Biochimica et biophysica acta · 2013Article
- Coupled electron and proton transfer reactions during the O→E transition in bovine cytochrome c oxidase.Biochimica et biophysica acta · 2012Review
- Expanding the view of proton pumping in cytochrome c oxidase through computer simulation.Biochimica et biophysica acta · 2012Article
- Differential effects of glutamate-286 mutations in the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides and the cytochrome bo(3) ubiquinol oxidase from Escherichia coli.Biochimica et biophysica acta · 2011Article
- Proton-transport mechanisms in cytochrome c oxidase revealed by studies of kinetic isotope effects.Biochimica et biophysica acta · 2011Article
- Alternative initial proton acceptors for the D pathway of Rhodobacter sphaeroides cytochrome c oxidase.Biochemistry · 2011Article
- Intricate role of water in proton transport through cytochrome c oxidase.Journal of the American Chemical Society · 2010Article
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4 authors at 2 institutions in 2 countries.
Funding
Abstract
Cytochrome c oxidase (CcO) is the terminal enzyme of the respiratory chain and couples energetically the reduction of oxygen to water to proton pumping across the membrane. The results from previous studies showed that proton pumping can be uncoupled from the O2-reduction reaction by replacement of one single residue, Asn-139 by Asp (N139D), located approximately 30 A from the catalytic site, in the D-proton pathway. The uncoupling was correlated with an increase in the pK(a) of an internal proton donor, Glu-286, from approximately 9.4 to >11. Here, we show that replacement of the acidic residue, Asp-132 by Asn in the N139D CcO (D132N/N139D double-mutant CcO) results in restoration of the Glu-286 pK(a) to the original value and recoupling of the proton pump during steady-state turnover. Furthermore, a kinetic investigation of the specific reaction steps in the D132N/N139D double-mutant CcO showed that proton pumping is sustained even if proton uptake from solution, through the D-pathway, is slowed. However, during single-turnover oxidation of the fully reduced CcO the P --> F transition, which does not involve electron transfer to the catalytic site, was not coupled to proton pumping. The results provide insights into the mechanism of proton pumping by CcO and the structural elements involved in this process.
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