Relationship between Proton Transport and Morphology of Perfluorosulfonic Acid Membranes: A Reactive Molecular Dynamics Approach

2018 ◽  
Vol 122 (22) ◽  
pp. 5922-5932 ◽  
Author(s):  
Takuya Mabuchi ◽  
Takashi Tokumasu
Keyword(s):  
Molecular Dynamics ◽  
Proton Transport ◽  
Perfluorosulfonic Acid ◽  
Reactive Molecular Dynamics ◽  
Perfluorosulfonic Acid Membranes

scholarly journals Multiscale Simulation Reveals Passive Proton Transport Through SERCA on the Microsecond Timescale

2020 ◽  
Author(s):  
Chenghan Li ◽  
Zhi Yue ◽  
L. Michel Espinoza-Fonseca ◽  
Gregory A. Voth
Keyword(s):  
Molecular Dynamics ◽  
Free Energy ◽  
Sarcoplasmic Reticulum ◽  
Binding Site ◽  
Proton Transport ◽  
Computational Study ◽  
Multiscale Simulation ◽  
Proton Pumping ◽  
Reactive Molecular Dynamics ◽  
Free Energy Sampling

ABSTRACTThe sarcoplasmic reticulum Ca2+-ATPase (SERCA) transports two Ca2+ ions from the cytoplasm to the reticulum lumen at the expense of ATP hydrolysis. In addition to transporting Ca2+, SERCA facilitates bidirectional proton transport across the sarcoplasmic reticulum to maintain the charge balance of the transport sites and to balance the charge deficit generated by the exchange of Ca2+. Previous studies have shown the existence of a transient water-filled pore in SERCA that connects the Ca2+-binding sites with the lumen, but the capacity of this pathway to sustain passive proton transport has remained unknown. In this study, we used the multiscale reactive molecular dynamics (MS-RMD) method and free energy sampling to quantify the free energy profile and timescale of the proton transport across this pathway while also explicitly accounting for the dynamically coupled hydration changes of the pore. We find that proton transport from the central binding site to the lumen has a microsecond timescale, revealing a novel passive cytoplasm-to-lumen proton flow beside the well-known inverse proton countertransport occurring in active Ca2+ transport. We propose that this proton transport mechanism is operational and serves as a functional conduit for passive proton transport across the sarcoplasmic reticulum.SIGNIFICANCEMultiscale reactive molecular dynamics combined with free energy sampling was applied to study proton transport through a transient water pore connecting the Ca2+-binding site to the lumen in SERCA. This is the first computational study of this large biomolecular system that treats the hydrated excess proton and its transport through water structures and amino acids explicitly. When also correctly accounting for the hydration fluctuations of the pore, it is found that a transiently hydrated channel can transport protons on a microsecond timescale. These results quantitatively support the hypothesis of the proton intake into the sarcoplasm via SERCA, in addition to the well-known proton pumping by SERCA to the cytoplasm along with Ca2+ transport.

A Reactive Molecular Dynamics Algorithm for Proton Transport in Aqueous Systems

2010 ◽  
Vol 114 (27) ◽  
pp. 11965-11976 ◽  
Author(s):  
Myvizhi Esai Selvan ◽  
David J. Keffer ◽  
Shengting Cui ◽  
Stephen J. Paddison
Keyword(s):  
Molecular Dynamics ◽  
Proton Transport ◽  
Aqueous Systems ◽  
Reactive Molecular Dynamics

Comparison of the Hydration and Diffusion of Protons in Perfluorosulfonic Acid Membranes with Molecular Dynamics Simulations

2008 ◽  
Vol 112 (42) ◽  
pp. 13273-13284 ◽  
Author(s):  
Shengting Cui ◽  
Junwu Liu ◽  
Myvizhi Esai Selvan ◽  
Stephen J. Paddison ◽  
David J. Keffer ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Perfluorosulfonic Acid ◽  
Perfluorosulfonic Acid Membranes ◽  
Dynamics Simulations ◽  
And Diffusion
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