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Cover Feature: Protein‐Assisted Formation and Stabilization of Catalytically Active Polyoxometalate Species (Chem. Eur. J. 40/2018)
Author(s) -
Vandebroek Laurens,
De Zitter Elke,
Ly Hong Giang Thi,
Conić Dragan,
Mihaylov Tzvetan,
Sap Annelies,
Proost Paul,
Pierloot Kristine,
Van Meervelt Luc,
ParacVogt Tatja.
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201802890
Subject(s) - polyoxometalate , monomer , hydrogen bond , lysozyme , chemistry , crystallography , catalysis , molecule , organic chemistry , biochemistry , polymer
The effect of the protein environment on the formation and stabilization of an elusive polyoxometalate (POM) species is described. The catalytically active monomeric POM, which is intrinsically unstable under physiological conditions, is observed in a co‐crystal structure with Hen Egg‐White Lysozyme. The protein environment plays a crucial role in assisting formation and stabilization of the monomeric POM via the low dielectric response at the protein surface and via electrostatic and water‐mediated hydrogen bonding interactions. More information can be found in the Full Paper by T. N. Parac‐Vogt, et al. on page 10099.