TUTCRIS - Tampereen teknillinen yliopisto

TUTCRIS

New perspectives on proton pumping in cellular respiration

Tutkimustuotos: Katsausartikkelivertaisarvioitu

Standard

New perspectives on proton pumping in cellular respiration. / Wikström, Mårten; Sharma, Vivek; Kaila, Ville R I; Hosler, Jonathan P.; Hummer, Gerhard.

julkaisussa: Chemical Reviews, Vuosikerta 115, Nro 5, 11.03.2015, s. 2196-2221.

Tutkimustuotos: Katsausartikkelivertaisarvioitu

Harvard

Wikström, M, Sharma, V, Kaila, VRI, Hosler, JP & Hummer, G 2015, 'New perspectives on proton pumping in cellular respiration', Chemical Reviews, Vuosikerta. 115, Nro 5, Sivut 2196-2221. https://doi.org/10.1021/cr500448t

APA

Wikström, M., Sharma, V., Kaila, V. R. I., Hosler, J. P., & Hummer, G. (2015). New perspectives on proton pumping in cellular respiration. Chemical Reviews, 115(5), 2196-2221. https://doi.org/10.1021/cr500448t

Vancouver

Wikström M, Sharma V, Kaila VRI, Hosler JP, Hummer G. New perspectives on proton pumping in cellular respiration. Chemical Reviews. 2015 maalis 11;115(5):2196-2221. https://doi.org/10.1021/cr500448t

Author

Wikström, Mårten ; Sharma, Vivek ; Kaila, Ville R I ; Hosler, Jonathan P. ; Hummer, Gerhard. / New perspectives on proton pumping in cellular respiration. Julkaisussa: Chemical Reviews. 2015 ; Vuosikerta 115, Nro 5. Sivut 2196-2221.

Bibtex - Lataa

@article{ba5fc4aa0fe348d682f71b84b1edf3f3,
title = "New perspectives on proton pumping in cellular respiration",
abstract = "Complexes I, III (cytochrome bc1), and IV (cytochrome c oxidase) of the respiratory chain employ fundamentally different mechanisms for redox-coupled proton pumping. In the Q-cycle of cytochrome bc1, charge separation is the result of electron transfer through the membrane, whereas the protons are shuttled across the membrane by a neutral quinol carrier, QH2. In this Q cycle, the mobile quinols get protonated on the N-side of the membrane and deprotonated on the P-side. Cytochrome bc1 thus transduces chemical energy into an electrochemical gradient through a redox loop, but is not a true proton pump in the sense of moving protonic charge through the protein directly against a pmf. By contrast, cytochrome c oxidase, the terminal enzyme of the respiratory chain, operates as a true proton pump. In cytochrome c oxidase (CcO), the pathways of chemical electron and proton fluxes intersect in the binuclear center, and the pathway of pumped protons passes close to the BNC as well. This spatial proximity of proton and electron pathways establishes the tight electrostatic interactions one might expect for a redox-coupled proton pump.",
author = "M{\aa}rten Wikstr{\"o}m and Vivek Sharma and Kaila, {Ville R I} and Hosler, {Jonathan P.} and Gerhard Hummer",
year = "2015",
month = "3",
day = "11",
doi = "10.1021/cr500448t",
language = "English",
volume = "115",
pages = "2196--2221",
journal = "Chemical Reviews",
issn = "0009-2665",
publisher = "AMER CHEMICAL SOC",
number = "5",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - New perspectives on proton pumping in cellular respiration

AU - Wikström, Mårten

AU - Sharma, Vivek

AU - Kaila, Ville R I

AU - Hosler, Jonathan P.

AU - Hummer, Gerhard

PY - 2015/3/11

Y1 - 2015/3/11

N2 - Complexes I, III (cytochrome bc1), and IV (cytochrome c oxidase) of the respiratory chain employ fundamentally different mechanisms for redox-coupled proton pumping. In the Q-cycle of cytochrome bc1, charge separation is the result of electron transfer through the membrane, whereas the protons are shuttled across the membrane by a neutral quinol carrier, QH2. In this Q cycle, the mobile quinols get protonated on the N-side of the membrane and deprotonated on the P-side. Cytochrome bc1 thus transduces chemical energy into an electrochemical gradient through a redox loop, but is not a true proton pump in the sense of moving protonic charge through the protein directly against a pmf. By contrast, cytochrome c oxidase, the terminal enzyme of the respiratory chain, operates as a true proton pump. In cytochrome c oxidase (CcO), the pathways of chemical electron and proton fluxes intersect in the binuclear center, and the pathway of pumped protons passes close to the BNC as well. This spatial proximity of proton and electron pathways establishes the tight electrostatic interactions one might expect for a redox-coupled proton pump.

AB - Complexes I, III (cytochrome bc1), and IV (cytochrome c oxidase) of the respiratory chain employ fundamentally different mechanisms for redox-coupled proton pumping. In the Q-cycle of cytochrome bc1, charge separation is the result of electron transfer through the membrane, whereas the protons are shuttled across the membrane by a neutral quinol carrier, QH2. In this Q cycle, the mobile quinols get protonated on the N-side of the membrane and deprotonated on the P-side. Cytochrome bc1 thus transduces chemical energy into an electrochemical gradient through a redox loop, but is not a true proton pump in the sense of moving protonic charge through the protein directly against a pmf. By contrast, cytochrome c oxidase, the terminal enzyme of the respiratory chain, operates as a true proton pump. In cytochrome c oxidase (CcO), the pathways of chemical electron and proton fluxes intersect in the binuclear center, and the pathway of pumped protons passes close to the BNC as well. This spatial proximity of proton and electron pathways establishes the tight electrostatic interactions one might expect for a redox-coupled proton pump.

UR - http://www.scopus.com/inward/record.url?scp=84924561761&partnerID=8YFLogxK

U2 - 10.1021/cr500448t

DO - 10.1021/cr500448t

M3 - Review Article

VL - 115

SP - 2196

EP - 2221

JO - Chemical Reviews

JF - Chemical Reviews

SN - 0009-2665

IS - 5

ER -