Spectroscopic/Computational Characterization and the X-ray Structure of the Adduct of the V<sup>IV</sup>O–Picolinato Complex with RNase A
Giarita Ferraro, Nicola Demitri, Luigi Vitale, Giuseppe Sciortino, Daniele Sanna, Valeria Ugone, Eugenio Garribba, Antonello Merlino
Abstract
-6-23-Δ enantiomer establishing an extended network of hydrogen bonds and van der Waals stabilizations. By increasing the pH around neutrality, with the deprotonation of histidine side chains, the binding of the V complex to His105 and His119 could occur, with that to His105 which should be preferred when compared to that to the catalytically important His119. The binding of the V compound affects the enzymatic activity of RNase A, but it does not alter its overall structure and stability.
Topics & Concepts
ChemistryMoietyRNase PImidazoleAdductStereochemistryHydrogen bondCircular dichroismCrystallographyCarboxylateElectrospray ionizationElectron paramagnetic resonanceProtonationHistidineMoleculeMass spectrometryEnzymeOrganic chemistryChromatographyRNABiochemistryPhysicsNuclear magnetic resonanceGeneIonVanadium and Halogenation ChemistryElectrochemical Analysis and ApplicationsChemical and Physical Properties in Aqueous Solutions