Redox-dependent proton translocation in cbb3 oxidase

Catarina Carvalheda Dos Santos, Andrei Pisliakov

Research output: Contribution to journalMeeting abstract

Abstract

Heme-copper oxidases (HCOs) couple the chemical energy released in reduction of oxygen to water, the final step of the respiratory chain, to the active proton translocation across the membrane, thus contributing to the establishment of a proton gradient, which is essential for ATP synthesis. Cbb3 (or C-type) cytochrome c oxidases are a highly divergent group and the least studied members of the HCO superfamily. They exhibit unique structural and functional features, and have an essential role in metabolism of clinically relevant human pathogens. The functioning mechanism of cbb3 oxidases, namely the proton transfer/pumping mechanism via a single proton channel, is still poorly understood. In this work we use a combination of computational tools to get atomic-level insights into the water dynamics and proton translocation in cbb3 oxidase. Recently we described the proton transfer pathways for the “chemical” and “pumped” protons, and proposed a redox-driven pumping mechanism (Carvalheda 2017 BBA-Bioenerg. 1858 396). Here we report the impact of redox changes in the binuclear centre on the proton pathways and protonation equilibria of key residues. Our results contribute to a better understanding of cbb3 mechanism and provide ideas for further experimental and computational studies.
Original languageEnglish
Pages (from-to)S258
JournalEuropean Biophysics Journal
Volume46
DOIs
Publication statusPublished - 2017
EventEuropean Biophysics Congress - Edinburgh, United Kingdom
Duration: 16 Jul 2017 → …

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Oxidation-Reduction
Protons
Heme
cbb3 oxidase
Water
Electron Transport Complex IV
Electron Transport
Adenosine Triphosphate
Oxygen
Membranes

Cite this

Carvalheda Dos Santos, Catarina ; Pisliakov, Andrei. / Redox-dependent proton translocation in cbb3 oxidase. In: European Biophysics Journal. 2017 ; Vol. 46. pp. S258.
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title = "Redox-dependent proton translocation in cbb3 oxidase",
abstract = "Heme-copper oxidases (HCOs) couple the chemical energy released in reduction of oxygen to water, the final step of the respiratory chain, to the active proton translocation across the membrane, thus contributing to the establishment of a proton gradient, which is essential for ATP synthesis. Cbb3 (or C-type) cytochrome c oxidases are a highly divergent group and the least studied members of the HCO superfamily. They exhibit unique structural and functional features, and have an essential role in metabolism of clinically relevant human pathogens. The functioning mechanism of cbb3 oxidases, namely the proton transfer/pumping mechanism via a single proton channel, is still poorly understood. In this work we use a combination of computational tools to get atomic-level insights into the water dynamics and proton translocation in cbb3 oxidase. Recently we described the proton transfer pathways for the “chemical” and “pumped” protons, and proposed a redox-driven pumping mechanism (Carvalheda 2017 BBA-Bioenerg. 1858 396). Here we report the impact of redox changes in the binuclear centre on the proton pathways and protonation equilibria of key residues. Our results contribute to a better understanding of cbb3 mechanism and provide ideas for further experimental and computational studies.",
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Redox-dependent proton translocation in cbb3 oxidase. / Carvalheda Dos Santos, Catarina; Pisliakov, Andrei.

In: European Biophysics Journal, Vol. 46, 2017, p. S258.

Research output: Contribution to journalMeeting abstract

TY - JOUR

T1 - Redox-dependent proton translocation in cbb3 oxidase

AU - Carvalheda Dos Santos, Catarina

AU - Pisliakov, Andrei

PY - 2017

Y1 - 2017

N2 - Heme-copper oxidases (HCOs) couple the chemical energy released in reduction of oxygen to water, the final step of the respiratory chain, to the active proton translocation across the membrane, thus contributing to the establishment of a proton gradient, which is essential for ATP synthesis. Cbb3 (or C-type) cytochrome c oxidases are a highly divergent group and the least studied members of the HCO superfamily. They exhibit unique structural and functional features, and have an essential role in metabolism of clinically relevant human pathogens. The functioning mechanism of cbb3 oxidases, namely the proton transfer/pumping mechanism via a single proton channel, is still poorly understood. In this work we use a combination of computational tools to get atomic-level insights into the water dynamics and proton translocation in cbb3 oxidase. Recently we described the proton transfer pathways for the “chemical” and “pumped” protons, and proposed a redox-driven pumping mechanism (Carvalheda 2017 BBA-Bioenerg. 1858 396). Here we report the impact of redox changes in the binuclear centre on the proton pathways and protonation equilibria of key residues. Our results contribute to a better understanding of cbb3 mechanism and provide ideas for further experimental and computational studies.

AB - Heme-copper oxidases (HCOs) couple the chemical energy released in reduction of oxygen to water, the final step of the respiratory chain, to the active proton translocation across the membrane, thus contributing to the establishment of a proton gradient, which is essential for ATP synthesis. Cbb3 (or C-type) cytochrome c oxidases are a highly divergent group and the least studied members of the HCO superfamily. They exhibit unique structural and functional features, and have an essential role in metabolism of clinically relevant human pathogens. The functioning mechanism of cbb3 oxidases, namely the proton transfer/pumping mechanism via a single proton channel, is still poorly understood. In this work we use a combination of computational tools to get atomic-level insights into the water dynamics and proton translocation in cbb3 oxidase. Recently we described the proton transfer pathways for the “chemical” and “pumped” protons, and proposed a redox-driven pumping mechanism (Carvalheda 2017 BBA-Bioenerg. 1858 396). Here we report the impact of redox changes in the binuclear centre on the proton pathways and protonation equilibria of key residues. Our results contribute to a better understanding of cbb3 mechanism and provide ideas for further experimental and computational studies.

U2 - 10.1007/s00249-017-1222-x

DO - 10.1007/s00249-017-1222-x

M3 - Meeting abstract

VL - 46

SP - S258

JO - European Biophysics Journal

JF - European Biophysics Journal

SN - 0175-7571

ER -