Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase

Abstract In cytochrome c oxidase (CytcO) reduction of O2 to water is linked to uptake of eight protons from the negative side of the membrane: four are substrate protons used to form water and four are pumped across the membrane. In bacterial oxidases, the substrate protons are taken up through the...

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Autores principales:	Markus L. Björck, Jóhanna Vilhjálmsdóttir, Andrew M. Hartley, Brigitte Meunier, Linda Näsvik Öjemyr, Amandine Maréchal, Peter Brzezinski
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7a5c6d85f7a14eecad7fea0c28fc7955
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spelling	oai:doaj.org-article:7a5c6d85f7a14eecad7fea0c28fc79552021-12-02T13:34:54ZProton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase10.1038/s41598-019-56648-92045-2322https://doaj.org/article/7a5c6d85f7a14eecad7fea0c28fc79552019-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-019-56648-9https://doaj.org/toc/2045-2322Abstract In cytochrome c oxidase (CytcO) reduction of O2 to water is linked to uptake of eight protons from the negative side of the membrane: four are substrate protons used to form water and four are pumped across the membrane. In bacterial oxidases, the substrate protons are taken up through the K and the D proton pathways, while the pumped protons are transferred through the D pathway. On the basis of studies with CytcO isolated from bovine heart mitochondria, it was suggested that in mitochondrial CytcOs the pumped protons are transferred though a third proton pathway, the H pathway, rather than through the D pathway. Here, we studied these reactions in S. cerevisiae CytcO, which serves as a model of the mammalian counterpart. We analyzed the effect of mutations in the D (Asn99Asp and Ile67Asn) and H pathways (Ser382Ala and Ser458Ala) and investigated the kinetics of electron and proton transfer during the reaction of the reduced CytcO with O2. No effects were observed with the H pathway variants while in the D pathway variants the functional effects were similar to those observed with the R. sphaeroides CytcO. The data indicate that the S. cerevisiae CytcO uses the D pathway for proton uptake and presumably also for proton pumping.Markus L. BjörckJóhanna VilhjálmsdóttirAndrew M. HartleyBrigitte MeunierLinda Näsvik ÖjemyrAmandine MaréchalPeter BrzezinskiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 9, Iss 1, Pp 1-8 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Markus L. Björck Jóhanna Vilhjálmsdóttir Andrew M. Hartley Brigitte Meunier Linda Näsvik Öjemyr Amandine Maréchal Peter Brzezinski Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase
description	Abstract In cytochrome c oxidase (CytcO) reduction of O2 to water is linked to uptake of eight protons from the negative side of the membrane: four are substrate protons used to form water and four are pumped across the membrane. In bacterial oxidases, the substrate protons are taken up through the K and the D proton pathways, while the pumped protons are transferred through the D pathway. On the basis of studies with CytcO isolated from bovine heart mitochondria, it was suggested that in mitochondrial CytcOs the pumped protons are transferred though a third proton pathway, the H pathway, rather than through the D pathway. Here, we studied these reactions in S. cerevisiae CytcO, which serves as a model of the mammalian counterpart. We analyzed the effect of mutations in the D (Asn99Asp and Ile67Asn) and H pathways (Ser382Ala and Ser458Ala) and investigated the kinetics of electron and proton transfer during the reaction of the reduced CytcO with O2. No effects were observed with the H pathway variants while in the D pathway variants the functional effects were similar to those observed with the R. sphaeroides CytcO. The data indicate that the S. cerevisiae CytcO uses the D pathway for proton uptake and presumably also for proton pumping.
format	article
author	Markus L. Björck Jóhanna Vilhjálmsdóttir Andrew M. Hartley Brigitte Meunier Linda Näsvik Öjemyr Amandine Maréchal Peter Brzezinski
author_facet	Markus L. Björck Jóhanna Vilhjálmsdóttir Andrew M. Hartley Brigitte Meunier Linda Näsvik Öjemyr Amandine Maréchal Peter Brzezinski
author_sort	Markus L. Björck
title	Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase
title_short	Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase
title_full	Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase
title_fullStr	Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase
title_full_unstemmed	Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase
title_sort	proton-transfer pathways in the mitochondrial s. cerevisiae cytochrome c oxidase
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/7a5c6d85f7a14eecad7fea0c28fc7955
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Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase

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