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• W2783005626 abstract "Enzyme immobilization with a nanostructure material can enhance its stability and facilitate reusability. However, the apparent activity is often compromised due to additional diffusion barriers and complex interactions with the substrates and solvent molecules. The present study elucidates the effects of the surface hydrophobicity of nano-confinement on CO2 diffusion to the active site of human carbonic anhydrase II (CA), an enzyme that is able to catalyze CO2 hydration at extremely high turnover rates. Using the Markov-state model in combination with coarse-grained molecular dynamics simulations, we demonstrate that a hydrophobic cage increases CO2 local density but hinders its diffusion towards the active site of CA under confinement. By contrast, a hydrophilic cage hinders CO2 adsorption but promotes its binding with CA. An optimal surface hydrophobicity can be identified to maximize both the CO2 occupation probability and the diffusion rate. The simulation results offer insight into understanding enzyme performance under nano-confinement and help us to advance broader applications of CA for CO2 absorption and recovery." @default.
• W2783005626 created "2018-01-26" @default.
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• W2783005626 date "2018-01-16" @default.
• W2783005626 modified "2023-10-14" @default.
• W2783005626 title "Markov-state model for CO₂ binding with carbonic anhydrase under confinement" @default.
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• W2783005626 doi "https://doi.org/10.1063/1.5003298" @default.
• W2783005626 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29352785" @default.
• W2783005626 hasPublicationYear "2018" @default.
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