Insights into the molecular mechanism of complex I from atomistic molecular dynamics simulations.

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Insights into the molecular mechanism of complex I from atomistic molecular dynamics simulations. / Sharma, Vivek; Kaila, Ville; Wikström, Mårten; Vattulainen, Ilpo Tapio; Rog, Tomasz.

European Biophysics Journal. 2015, Conference abstract.

Tutkimustuotos › › vertaisarvioitu

Harvard

Sharma, V, Kaila, V, Wikström, M, Vattulainen, IT & Rog, T 2015, Insights into the molecular mechanism of complex I from atomistic molecular dynamics simulations. European Biophysics Journal.

APA

Sharma, V., Kaila, V., Wikström, M., Vattulainen, I. T., & Rog, T. (2015). Insights into the molecular mechanism of complex I from atomistic molecular dynamics simulations. European Biophysics Journal.

Vancouver

Sharma V, Kaila V, Wikström M, Vattulainen IT, Rog T. Insights into the molecular mechanism of complex I from atomistic molecular dynamics simulations. 2015.

Author

Sharma, Vivek ; Kaila, Ville ; Wikström, Mårten ; Vattulainen, Ilpo Tapio ; Rog, Tomasz. / Insights into the molecular mechanism of complex I from atomistic molecular dynamics simulations. 2015. European Biophysics Journal.

Bibtex - Lataa

@misc{23aa26496e844de8bb0f242e16dc5edd,

title = "Insights into the molecular mechanism of complex I from atomistic molecular dynamics simulations.",

abstract = "Complex I (NADH:quinone oxidoreductase) is the first elec-tron acceptor in the respiratory chains of mitochondria andmany bacteria. It catalyzes the reduction of quinone (Q),which is coupled to the proton pumping across the mem-brane. The redox reactions in the hydrophilic domain, andproton pumping in the membrane domain of the enzyme arespatially as well as temporally separated, and how the twoare coupled remains unclear. In order to shed light on theearly reactions of the catalytic cycle of complex I, we haveperformed atomistic classical molecular dynamics (MD) sim-ulations on the entire structure of complex I fromThermusthermophilus[1], immersed in a lipid-solvent environmentcomprising ca. 1 million atoms. MD simulations (∼100 ns)in different redox and protonation states of Q show that thelong-range redox coupled proton pumping in complex I isactivated by a combination of electrostatic interactions andconformational transitions [2].",

author = "Vivek Sharma and Ville Kaila and M{\aa}rten Wikstr{\"o}m and Vattulainen, {Ilpo Tapio} and Tomasz Rog",

note = "xposter",

year = "2015",

language = "English",

volume = "44",

publisher = "European Biophysics Journal",

type = "Other",

}

RIS (suitable for import to EndNote) - Lataa

TY - GEN

T1 - Insights into the molecular mechanism of complex I from atomistic molecular dynamics simulations.

AU - Sharma, Vivek

AU - Kaila, Ville

AU - Wikström, Mårten

AU - Vattulainen, Ilpo Tapio

AU - Rog, Tomasz

N1 - xposter

PY - 2015

Y1 - 2015

N2 - Complex I (NADH:quinone oxidoreductase) is the first elec-tron acceptor in the respiratory chains of mitochondria andmany bacteria. It catalyzes the reduction of quinone (Q),which is coupled to the proton pumping across the mem-brane. The redox reactions in the hydrophilic domain, andproton pumping in the membrane domain of the enzyme arespatially as well as temporally separated, and how the twoare coupled remains unclear. In order to shed light on theearly reactions of the catalytic cycle of complex I, we haveperformed atomistic classical molecular dynamics (MD) sim-ulations on the entire structure of complex I fromThermusthermophilus[1], immersed in a lipid-solvent environmentcomprising ca. 1 million atoms. MD simulations (∼100 ns)in different redox and protonation states of Q show that thelong-range redox coupled proton pumping in complex I isactivated by a combination of electrostatic interactions andconformational transitions [2].

AB - Complex I (NADH:quinone oxidoreductase) is the first elec-tron acceptor in the respiratory chains of mitochondria andmany bacteria. It catalyzes the reduction of quinone (Q),which is coupled to the proton pumping across the mem-brane. The redox reactions in the hydrophilic domain, andproton pumping in the membrane domain of the enzyme arespatially as well as temporally separated, and how the twoare coupled remains unclear. In order to shed light on theearly reactions of the catalytic cycle of complex I, we haveperformed atomistic classical molecular dynamics (MD) sim-ulations on the entire structure of complex I fromThermusthermophilus[1], immersed in a lipid-solvent environmentcomprising ca. 1 million atoms. MD simulations (∼100 ns)in different redox and protonation states of Q show that thelong-range redox coupled proton pumping in complex I isactivated by a combination of electrostatic interactions andconformational transitions [2].

M3 - Other contribution

VL - 44

PB - European Biophysics Journal

ER -

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