Redox-coupled proton transfer in the respiratory complex I

V. Kaila, A. P. Gamiz-Hernandez, V. Sharma, J. Warnau, A Jussupow, M Johansson, G Belevich, M. Verkhovskaya, G. Hummer, M. Wikström

Redox-coupled proton transfer in the respiratory complex I

V. Kaila, A. P. Gamiz-Hernandez, V. Sharma, J. Warnau, A Jussupow, M Johansson, G Belevich, M. Verkhovskaya, G. Hummer, M. Wikström

Research output: Other contribution › peer-review

Abstract

Complex I functions as a redox-driven proton pump in the
aerobic respiratory chains of bacteria and eukaryotes. Re-
markably, the electron transfer domain of complex I is sepa-
rated by
ca
. 200
̊
A from the most distant proton pathways.
To understand the molecular mechanism of this biomolecular
machine, we perform here large-scale classical and quantum
molecular simulations, and site-directed mutagenesis experi-
ments, to study how the quinone reduction triggers the func-
tion of the proton pump. We find that coupled electrostatic,
conformational, and hydration changes are central for estab-
lishing the long-range energy coupling in complex I.

Original language	English
Type	Conference abstract
Media of output	Poster
Publisher	European Biophysics Journal
Volume	44
Publication status	Published - 2015

Cite this

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title = "Redox-coupled proton transfer in the respiratory complex I",

abstract = "Complex I functions as a redox-driven proton pump in the aerobic respiratory chains of bacteria and eukaryotes. Re- markably, the electron transfer domain of complex I is sepa- rated by ca . 200 ̊ A from the most distant proton pathways. To understand the molecular mechanism of this biomolecular machine, we perform here large-scale classical and quantum molecular simulations, and site-directed mutagenesis experi- ments, to study how the quinone reduction triggers the func- tion of the proton pump. We find that coupled electrostatic, conformational, and hydration changes are central for estab- lishing the long-range energy coupling in complex I.",

author = "Vivek Sharma and \{V. Kaila, A. P. Gamiz-Hernandez, V. Sharma, J. Warnau, A Jussupow, M Johansson, G Belevich, M. Verkhovskaya, G. Hummer, M. Wikstr{\"o}m\}",

note = "xposter",

year = "2015",

language = "English",

volume = "44",

publisher = "European Biophysics Journal",

type = "Other",

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TY - GEN

T1 - Redox-coupled proton transfer in the respiratory complex I

AU - Sharma, Vivek

AU - V. Kaila, A. P. Gamiz-Hernandez, V. Sharma, J. Warnau, A Jussupow, M Johansson, G Belevich, M. Verkhovskaya, G. Hummer, M. Wikström

N1 - xposter

PY - 2015

Y1 - 2015

N2 - Complex I functions as a redox-driven proton pump in the aerobic respiratory chains of bacteria and eukaryotes. Re- markably, the electron transfer domain of complex I is sepa- rated by ca . 200 ̊ A from the most distant proton pathways. To understand the molecular mechanism of this biomolecular machine, we perform here large-scale classical and quantum molecular simulations, and site-directed mutagenesis experi- ments, to study how the quinone reduction triggers the func- tion of the proton pump. We find that coupled electrostatic, conformational, and hydration changes are central for estab- lishing the long-range energy coupling in complex I.

AB - Complex I functions as a redox-driven proton pump in the aerobic respiratory chains of bacteria and eukaryotes. Re- markably, the electron transfer domain of complex I is sepa- rated by ca . 200 ̊ A from the most distant proton pathways. To understand the molecular mechanism of this biomolecular machine, we perform here large-scale classical and quantum molecular simulations, and site-directed mutagenesis experi- ments, to study how the quinone reduction triggers the func- tion of the proton pump. We find that coupled electrostatic, conformational, and hydration changes are central for estab- lishing the long-range energy coupling in complex I.

M3 - Other contribution

VL - 44

PB - European Biophysics Journal

ER -

Redox-coupled proton transfer in the respiratory complex I

Abstract

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