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The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase

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The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase. / Sharma, Vivek; Wikström, Mårten.

In: Biochimica et Biophysica Acta: Bioenergetics, Vol. 1857, No. 8, 08.2016, p. 1111-1115.

Research output: Contribution to journalArticleScientificpeer-review

Harvard

Sharma, V & Wikström, M 2016, 'The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase', Biochimica et Biophysica Acta: Bioenergetics, vol. 1857, no. 8, pp. 1111-1115. https://doi.org/10.1016/j.bbabio.2016.02.008

APA

Sharma, V., & Wikström, M. (2016). The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase. Biochimica et Biophysica Acta: Bioenergetics, 1857(8), 1111-1115. https://doi.org/10.1016/j.bbabio.2016.02.008

Vancouver

Author

Sharma, Vivek ; Wikström, Mårten. / The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase. In: Biochimica et Biophysica Acta: Bioenergetics. 2016 ; Vol. 1857, No. 8. pp. 1111-1115.

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@article{51be6eb6bc234212a692316a25a16413,
title = "The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase",
abstract = "The active site of cytochrome c oxidase (CcO) comprises an oxygen-binding heme, a nearby copper ion (CuB), and a tyrosine residue that is covalently linked to one of the histidine ligands of CuB. Two proton-conducting pathways are observed in CcO, namely the D- and the K-channels, which are used to transfer protons either to the active site of oxygen reduction (substrate protons) or for pumping. Proton transfer through the D-channel is very fast, and its role in efficient transfer of both substrate and pumped protons is well established. However, it has not been fully clear why a separate K-channel is required, apparently for the supply of substrate protons only. In this work, we have analysed the available experimental and computational data, based on which we provide new perspectives on the role of the K-channel. Our analysis suggests that proton transfer in the K-channel may be gated by the protonation state of the active-site tyrosine (Tyr244) and that the neutral radical form of this residue has a more general role in the CcO mechanism than thought previously. This article is part of a Special Issue entitled 'EBEC 2016: 19th European Bioenergetics Conference, Riva del Garda, Italy, July 2-6, 2016', edited by Prof. Paolo Bernardi.",
keywords = "Electron transfer, Neutral tyrosyl radical, Proton pumping",
author = "Vivek Sharma and M{\aa}rten Wikstr{\"o}m",
year = "2016",
month = "8",
doi = "10.1016/j.bbabio.2016.02.008",
language = "English",
volume = "1857",
pages = "1111--1115",
journal = "Biochimica et Biophysica Acta: Bioenergetics",
issn = "0005-2728",
publisher = "Elsevier",
number = "8",

}

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TY - JOUR

T1 - The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase

AU - Sharma, Vivek

AU - Wikström, Mårten

PY - 2016/8

Y1 - 2016/8

N2 - The active site of cytochrome c oxidase (CcO) comprises an oxygen-binding heme, a nearby copper ion (CuB), and a tyrosine residue that is covalently linked to one of the histidine ligands of CuB. Two proton-conducting pathways are observed in CcO, namely the D- and the K-channels, which are used to transfer protons either to the active site of oxygen reduction (substrate protons) or for pumping. Proton transfer through the D-channel is very fast, and its role in efficient transfer of both substrate and pumped protons is well established. However, it has not been fully clear why a separate K-channel is required, apparently for the supply of substrate protons only. In this work, we have analysed the available experimental and computational data, based on which we provide new perspectives on the role of the K-channel. Our analysis suggests that proton transfer in the K-channel may be gated by the protonation state of the active-site tyrosine (Tyr244) and that the neutral radical form of this residue has a more general role in the CcO mechanism than thought previously. This article is part of a Special Issue entitled 'EBEC 2016: 19th European Bioenergetics Conference, Riva del Garda, Italy, July 2-6, 2016', edited by Prof. Paolo Bernardi.

AB - The active site of cytochrome c oxidase (CcO) comprises an oxygen-binding heme, a nearby copper ion (CuB), and a tyrosine residue that is covalently linked to one of the histidine ligands of CuB. Two proton-conducting pathways are observed in CcO, namely the D- and the K-channels, which are used to transfer protons either to the active site of oxygen reduction (substrate protons) or for pumping. Proton transfer through the D-channel is very fast, and its role in efficient transfer of both substrate and pumped protons is well established. However, it has not been fully clear why a separate K-channel is required, apparently for the supply of substrate protons only. In this work, we have analysed the available experimental and computational data, based on which we provide new perspectives on the role of the K-channel. Our analysis suggests that proton transfer in the K-channel may be gated by the protonation state of the active-site tyrosine (Tyr244) and that the neutral radical form of this residue has a more general role in the CcO mechanism than thought previously. This article is part of a Special Issue entitled 'EBEC 2016: 19th European Bioenergetics Conference, Riva del Garda, Italy, July 2-6, 2016', edited by Prof. Paolo Bernardi.

KW - Electron transfer

KW - Neutral tyrosyl radical

KW - Proton pumping

U2 - 10.1016/j.bbabio.2016.02.008

DO - 10.1016/j.bbabio.2016.02.008

M3 - Article

VL - 1857

SP - 1111

EP - 1115

JO - Biochimica et Biophysica Acta: Bioenergetics

JF - Biochimica et Biophysica Acta: Bioenergetics

SN - 0005-2728

IS - 8

ER -