Dataset Information

Dynamics and Surface Propensity of H⁺ and OH^- within Rigid Interfacial Water: Implications for Electrocatalysis.

ABSTRACT: Facile solvent reorganization promoting ion transfer across the solid-liquid interface is considered a prerequisite for efficient electrocatalysis. We provide first-principles insight into this notion by examining water self-ion dynamics at a highly rigid NaCl(100)-water interface. Through extensive density functional theory molecular dynamics simulations, we demonstrate for both acidic and alkaline solutions that Grotthuss dynamics is not impeded by a rigid water structure. Conversely, decreased proton transfer barriers and a striking propensity of H₃O⁺ and OH^- for stationary interfacial water are found. Differences in the ideal hydration structure of the ions, however, distinguish their behavior at the water contact layer. While hydronium can maintain its optimal solvation, the preferentially hypercoordinated hydroxide is repelled from the immediate vicinity of the surface due to interfacial coordination reduction. This has implications for alkaline hydrogen electrosorption in which the formation of undercoordinated OH^- at the surface is proposed to contribute to the observed sluggish kinetics.

SUBMITTER: Kronberg R

PROVIDER: S-EPMC8543677 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Dynamics and Surface Propensity of H<sup>+</sup> and OH<sup>-</sup> within Rigid Interfacial Water: Implications for Electrocatalysis.

Kronberg Rasmus R Laasonen Kari K

The journal of physical chemistry letters 20211012 41

Facile solvent reorganization promoting ion transfer across the solid-liquid interface is considered a prerequisite for efficient electrocatalysis. We provide first-principles insight into this notion by examining water self-ion dynamics at a highly rigid NaCl(100)-water interface. Through extensive density functional theory molecular dynamics simulations, we demonstrate for both acidic and alkaline solutions that Grotthuss dynamics is not impeded by a rigid water structure. Conversely, decrease ...[more]

PMID: 34636561

Similar Datasets

Project description:BACKGROUND: Protein-protein docking is an in silico method to predict the formation of protein complexes. Due to limited computational resources, the protein-protein docking approach has been developed under the assumption of rigid docking, in which one of the two protein partners remains rigid during the protein associations and water contribution is ignored or implicitly presented. Despite obtaining a number of acceptable complex predictions, it seems to-date that most initial rigid docking algorithms still find it difficult or even fail to discriminate successfully the correct predictions from the other incorrect or false positive ones. To improve the rigid docking results, re-ranking is one of the effective methods that help re-locate the correct predictions in top high ranks, discriminating them from the other incorrect ones. RESULTS: Our results showed that the IFACEwat increased both the numbers of the near-native structures and improved their ranks as compared to the initial rigid docking ZDOCK3.0.2. In fact, the IFACEwat achieved a success rate of 83.8% for Antigen/Antibody complexes, which is 10% better than ZDOCK3.0.2. As compared to another re-ranking technique ZRANK, the IFACEwat obtains success rates of 92.3% (8% better) and 90% (5% better) respectively for medium and difficult cases. When comparing with the latest published re-ranking method F2Dock, the IFACEwat performed equivalently well or even better for several Antigen/Antibody complexes. CONCLUSIONS: With the inclusion of interfacial water, the IFACEwat improves mostly results of the initial rigid docking, especially for Antigen/Antibody complexes. The improvement is achieved by explicitly taking into account the contribution of water during the protein interactions, which was ignored or not fully presented by the initial rigid docking and other re-ranking techniques. In addition, the IFACEwat maintains sufficient computational efficiency of the initial docking algorithm, yet improves the ranks as well as the number of the near native structures found. As our implementation so far targeted to improve the results of ZDOCK3.0.2, and particularly for the Antigen/Antibody complexes, it is expected in the near future that more implementations will be conducted to be applicable for other initial rigid docking algorithms.

Dataset Information

Dynamics and Surface Propensity of H⁺ and OH^- within Rigid Interfacial Water: Implications for Electrocatalysis.

Publications

Dynamics and Surface Propensity of H<sup>+</sup> and OH<sup>-</sup> within Rigid Interfacial Water: Implications for Electrocatalysis.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

Dynamics and Surface Propensity of H+ and OH- within Rigid Interfacial Water: Implications for Electrocatalysis.

Publications

Dynamics and Surface Propensity of H<sup>+</sup> and OH<sup>-</sup> within Rigid Interfacial Water: Implications for Electrocatalysis.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dynamics and Surface Propensity of H⁺ and OH^- within Rigid Interfacial Water: Implications for Electrocatalysis.