ArticleProceedings of the National Academy of Sciences of the United States of America2013
Role of aspartate 132 at the orifice of a proton pathway in cytochrome c oxidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- A Buried Water Network Modulates the Activity of theAntioxidants (Basel, Switzerland) · 2023Article
- Structure and Mechanism of Respiratory III-IV Supercomplexes in Bioenergetic Membranes.Chemical reviews · 2021Review
- Structural changes at the surface of cytochrome c oxidase alter the proton-pumping stoichiometry.Biochimica et biophysica acta. Bioenergetics · 2020Article
- Cavity hydration dynamics in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.Journal of biochemistry · 2016Article
- Analyzing the electrogenicity of cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Microscopic basis for kinetic gating in Cytochrome c oxidase: insights from QM/MM analysis.Chemical science · 2015Article
- Assembly of nonheme Mn/Fe active sites in heterodinuclear metalloproteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- Philosophy of voltage-gated proton channels.Journal of the Royal Society, Interface · 2014Review
- Peregrination of the selectivity filter delineates the pore of the human voltage-gated proton channel hHV1.The Journal of general physiology · 2013Article
- Single mutations that redirect internal proton transfer in the ba3 oxidase from Thermus thermophilus.Biochemistry · 2013Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Proton transfer across biological membranes underpins central processes in biological systems, such as energy conservation and transport of ions and molecules. In the membrane proteins involved in these processes, proton transfer takes place through specific pathways connecting the two sides of the membrane via control elements within the protein. It is commonly believed that acidic residues are required near the orifice of such proton pathways to facilitate proton uptake. In cytochrome c oxidase, one such pathway starts near a conserved Asp-132 residue. Results from earlier studies have shown that replacement of Asp-132 by, e.g., Asn, slows proton uptake by a factor of ∼5,000. Here, we show that proton uptake at full speed (∼10(4) s(-1)) can be restored in the Asp-132-Asn oxidase upon introduction of a second structural modification further inside the pathway (Asn-139-Thr) without compensating for the loss of the negative charge. This proton-uptake rate was insensitive to Zn(2+) addition, which in the wild-type cytochrome c oxidase slows the reaction, indicating that Asp-132 is required for Zn(2+) binding. Furthermore, in the absence of Asp-132 and with Thr at position 139, at high pH (>9), proton uptake was significantly accelerated. Thus, the data indicate that Asp-132 is not strictly required for maintaining rapid proton uptake. Furthermore, despite the rapid proton uptake in the Asn-139-Thr/Asp-132-Asn mutant cytochrome c oxidase, proton pumping was impaired, which indicates that the segment around these residues is functionally linked to pumping.
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