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Role of aspartate 132 at the orifice of a proton pathway in cytochrome c oxidase
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2013 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 110, no 22, 8912-8917 p.Article in journal (Refereed) Published
Abstract [en]

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 similar to 5,000. Here, we show that proton uptake at full speed (similar to 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 Zn2+ addition, which in the wildtype cytochrome c oxidase slows the reaction, indicating that Asp-132 is required for Zn2+ 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.

Place, publisher, year, edition, pages
2013. Vol. 110, no 22, 8912-8917 p.
Keyword [en]
cytochrome aa3, electron transfer, metalloprotein, respiration, transporter
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-92663DOI: 10.1073/pnas.1303954110ISI: 000320500000049OAI: oai:DiVA.org:su-92663DiVA: diva2:640776
Note

AuthorCount:5;

Available from: 2013-08-14 Created: 2013-08-14 Last updated: 2017-12-06Bibliographically approved

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