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• W4313592031 startingPage "014002" @default.
• W4313592031 abstract "Abstract Human carbonic anhydrase (CA) metalloenzymes utilize a Zn 2+ -containing active site to catalyze the interconversion of carbon dioxide to bicarbonate. The Zn 2+ ion may be replaced with other divalent transition metals, though the catalytic efficiency of the enzyme will be reduced. In this work, quantum mechanical cluster models of the active site are used to map the reaction profile for the hydration mechanism of carbon dioxide. The Lipscomb proton transfer and Lindskog rotation mechanisms were examined for the native Zn 2+ -enzyme along with variants where the metal was substituted with Cd 2+ , Ni 2+ , Fe 2+ , and Fe 3+ . The findings highlight the impact the metal coordination geometry has on the reaction profile. The results also suggest Fe 2+ , which is the functional metal for a prototypical CA of an anaerobic bacterium, might also be functional for human CA if cultured within an anaerobic environment." @default.
• W4313592031 created "2023-01-06" @default.
• W4313592031 creator A5045441223 @default.
• W4313592031 creator A5078787564 @default.
• W4313592031 date "2023-01-26" @default.
• W4313592031 modified "2023-10-16" @default.
• W4313592031 title "QM-cluster model study of CO₂ hydration mechanisms in metal-substituted human carbonic anhydrase II" @default.
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• W4313592031 doi "https://doi.org/10.1088/2516-1075/acb02c" @default.
• W4313592031 hasPublicationYear "2023" @default.
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