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Article Dans Une Revue Chemistry - A European Journal Année : 2015

Structural characterization of the complex between hen egg-white lysozyme and Zr$^{IV}$ -Substituted Keggin polyoxometalate as artificial protease

Résumé

Successful co-crystallization of a noncovalent complex between hen egg-white lysozyme (HEWL) and the monomeric Zr$^{IV}$-substituted Keggin polyoxometalate (POM) (Zr1K1), (Et$_2$NH$_2$)$_3$ [Zr(PW$_{11}$O$_{39}$)] (1), has been achieved, and its single-crystal X-ray structure has been determined. The dimeric Zr$^{IV}$-substituted Keggin-type polyoxometalate (Zr1K2), (Et$_2$NH$_2$)$_{10}$[Zr(PW$_{11}$O$_{39}$)$_2$] (2), has been previously shown to exhibit remarkable selectivity towards HEWL hydrolysis. The reported X-ray structure shows that the hydrolytically active Zr$^{IV}$-substituted Keggin POM exists as a monomeric species. Prior to hydrolysis, this monomer interacts with HEWL in the vicinity of the previously identified cleavage sites found at Trp28-Val29 and Asn44-Arg45, through water-mediated H-bonding and electrostatic interactions. Three binding sites are observed at the interface of the negatively charged Keggin POM and the positively charged regions of HEWL at: 1) Gly16, Tyr20, and Arg21; 2) Asn44, Arg45, and Asn46; and 3) Arg128.

Dates et versions

hal-03513233 , version 1 (05-01-2022)

Identifiants

Citer

Annelies Sap, Elke de Zitter, Luc Van meervelt, Tatjana N. Parac-Vogt. Structural characterization of the complex between hen egg-white lysozyme and Zr$^{IV}$ -Substituted Keggin polyoxometalate as artificial protease. Chemistry - A European Journal, 2015, 21 (33), pp.11692-11695. ⟨10.1002/chem.201501998⟩. ⟨hal-03513233⟩
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