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• W2095094632 abstract "In vanadium haloperoxidases, vanadate as the prosthetic group is fixed in the active site cavity by solely one covalent bond to a histidine residue and embedded in an environment of hydrogen bonds. Structural similarities between the active sites of vanadium haloperoxidases and some acid phosphatases are evident. Along this line, an important question is concerned with the role of the protein environment via supramolecular interactions for both structure and function of the related enzymatic systems. In this context, the relevance of cis-dioxovanadium(V) complexes with the versatile tridentate N-salicylidenehydrazide ligand system as models is discussed." @default.
• W2095094632 created "2016-06-24" @default.
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• W2095094632 date "2003-02-01" @default.
• W2095094632 modified "2023-10-16" @default.
• W2095094632 title "Supramolecular interactions of vanadate species: vanadium(V) complexes with N-salicylidenehydrazides as versatile models" @default.
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• W2095094632 doi "https://doi.org/10.1016/s0010-8545(02)00228-x" @default.
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