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  • Title: Dioxygen, an unexpected carbonic anhydrase ligand.
    Author: Ferraroni M, Gaspari R, Scozzafava A, Cavalli A, Supuran CT.
    Journal: J Enzyme Inhib Med Chem; 2018 Dec; 33(1):999-1005. PubMed ID: 29806484.
    Abstract:
    Carbonic anhydrases (CAs, EC 4.2.1.1) are ubiquitous metalloenzymes, grouped into seven different classes, which catalyze the reaction of CO2 hydration to bicarbonate and protons. All of the fifteen human isoforms reported to date belong to the α-class and contain zinc as a cofactor. The structure of human Zn,Cu-CA II has been solved which contains a copper ion bound at its N-terminal, coordinated to His4 and His64. In the active site a dioxygen molecule is coordinated to the zinc ion. Since dioxygen is a rather unexpected CA ligand, molecular dynamics (MD) simulations were performed which suggested a superoxide character of the zinc bound O2.
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