Dataset Information

Hydrogen bond unlocking-driven pore structure control for shifting multi-component gas separation function.

ABSTRACT: Purification of ethylene (C₂H₄) as the most extensive and output chemical, from complex multi-components is of great significance but highly challenging. Herein we demonstrate that precise pore structure tuning by controlling the network hydrogen bonds in two highly-related porous coordination networks can shift the efficient C₂H₄ separation function from C₂H₂/C₂H₄/C₂H₆ ternary mixture to CO₂/C₂H₂/C₂H₄/C₂H₆ quaternary mixture system. Single-crystal X-ray diffraction revealed that the different amino groups on the triazolate ligands resulted in the change of the hydrogen bonding in the host network, which led to changes in the pore shape and pore chemistry. Gas adsorption isotherms, adsorption kinetics and gas-loaded crystal structure analysis indicated that the coordination network Zn-fa-atz (2) weakened the affinity for three C2 hydrocarbons synchronously including C₂H₄ but enhanced the CO₂ adsorption due to the optimized CO₂-host interaction and the faster CO₂ diffusion, leading to effective C₂H₄ production from the CO₂/C₂H₂/C₂H₄/C₂H₆ mixture in one step based on the experimental and simulated breakthrough data. Moreover, it can be shaped into spherical pellets with maintained porosity and separation performance.

SUBMITTER: Yang R

PROVIDER: S-EPMC10821866 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature

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Hydrogen bond unlocking-driven pore structure control for shifting multi-component gas separation function.

Yang Rong R Wang Yu Y Cao Jian-Wei JW Ye Zi-Ming ZM Pham Tony T Forrest Katherine A KA Krishna Rajamani R Chen Hongwei H Li Libo L Ling Bo-Kai BK Zhang Tao T Gao Tong T Jiang Xue X Xu Xiang-Ou XO Ye Qian-Hao QH Chen Kai-Jie KJ

Nature communications 20240127 1

Purification of ethylene (C2H4) as the most extensive and output chemical, from complex multi-components is of great significance but highly challenging. Herein we demonstrate that precise pore structure tuning by controlling the network hydrogen bonds in two highly-related porous coordination networks can shift the efficient C2H4 separation function from C2H2/C2H4/C2H6 ternary mixture t ...[more]

PMID: 38280865

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Project description:Antibiotic resistance is a global health problem in which mutations occurring in functional proteins render drugs ineffective. The working mechanisms of the arising mutants are seldom apparent; a methodology to decipher these mechanisms systematically would render devising therapies to control the arising mutational pathways possible. Here we utilize Cα-Cβ bond vector relaxations obtained from moderate length MD trajectories to determine conduits for functionality of the resistance conferring mutants of Escherichia coli dihydrofolate reductase. We find that the whole enzyme is synchronized to the motions of the substrate, irrespective of the mutation introducing gain-of-function or loss-of function. The total coordination of the motions suggests changes in the hydrogen bond dynamics with respect to the wild type as a possible route to determine and classify the mode-of-action of individual mutants. As a result, nine trimethoprim-resistant point mutations arising frequently in evolution experiments are categorized. One group of mutants that display the largest occurrence (L28R, W30G) work directly by modifying the dihydrofolate binding region. Conversely, W30R works indirectly by the formation of the E139-R30 salt bridge which releases energy resulting from tight binding by distorting the binding cavity. A third group (D27E, F153S, I94L) arising as single, resistance invoking mutants in evolution experiment trajectories allosterically and dynamically affects a hydrogen bonding motif formed at residues 59-69-71 which in turn modifies the binding site dynamics. The final group (I5F, A26T, R98P) consists of those mutants that have properties most similar to the wild type; these only appear after one of the other mutants is fixed on the protein structure and therefore display clear epistasis. Thus, we show that the binding event is governed by the entire enzyme dynamics while the binding site residues play gating roles. The adjustments made in the total enzyme in response to point mutations are what make quantifying and pinpointing their effect a hard problem. Here, we show that hydrogen bond dynamics recorded on sub-μs time scales provide the necessary fingerprints to decipher the various mechanisms at play.

Dataset Information

Hydrogen bond unlocking-driven pore structure control for shifting multi-component gas separation function.

Publications

Hydrogen bond unlocking-driven pore structure control for shifting multi-component gas separation function.

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