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    Transformation of 5-chloro- and 5-bromo-2-cyanopyridine to amides and iminonitriles at the Mo(IV) center

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    The reaction of K3Na[Mo(CN)4O2]6H2OK_{3}Na[Mo(CN)_{4}O_{2}]·6H_{2}O complex with 5-chloro-2-cyanopyridine (5cl2py) and 5-bromo-2-cyanopyridine (5br2py), results in isolation of 4 new compounds, which were characterized by single X-ray crystal structure measurements, elemental analyses, IR and UV-Vis spectroscopy methods. Dimeric complex with the formula (PPh4)4[Mo(CN)3O(μCN)Mo(CN)4(H2O)]5cl2py5H2OEtOH(PPh_{4})_{4}[Mo(CN)_{3}O(μ-CN)Mo(CN)_{4}(H_{2}O)]·5cl2py·5H_{2}O·EtOH was isolated for the first time. The exchange of cyanido ligands for bidentate organic ligands, in this type of complexes, is largely pH dependent. Careful control of the reaction environment made it possible to obtain a modified organic ligand in which the nitrile group was hydrolyzed to the amide group (pH ca 8), or transformed, due to presence of cyanides in solution, to imino(5-chloropyridin-2-yl)acetonitrile (5cl2pya) or imino(5-bromopyridin-2-yl)acetonitrile (5br2pya), respectively. Two complexes with the formulas (PPh4)2[Mo(CN)3O(5cl2pya)]5cl2py(PPh_{4})_{2}[Mo(CN)_{3}O(5cl2pya)]·5cl2py and (PPh4)2[Mo(CN)3O(5br2pya)]5br2py(PPh_{4})_{2}[Mo(CN)_{3}O(5br2pya)]·5br2py (pH ca 10) were isolated. In these compounds, the 5cl2pya (or 5br2pya) was coordinated to the metal center as N,N-donating ligand, in which the modification of the nitrile group is discussed in detail in the paper

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    Changes in the structure and thermal properties of feather keratin induced by L-Cys extraction followed by enzymatic hydrolysis

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    Feather waste was valorised into bioactive peptides by extracting high-purity L-Cys–urea solution, followed by enzymatic hydrolysis with commercial proteases selected for their catalytic efficiency. The extraction reduced the α-helix content in favor of the β-sheet leading to less ordered crystal structures as ATR FT-IR and the XRD analyses revealed. These structural changes decreased keratin's thermal stability, resulting in its slower yet more gradual decomposition, as TGA and DSC results showed. The hydrolysis with trypsin, chymotrypsin, pepsin and subtilisin altered the secondary structure and thermal stability of extracted keratin, with changes depending on enzyme specificity. All hydrolysates showed the preserved amide features but reduced α-helix and β-sheet content and crystallinity. Subtilisin induced the most profound structural and molecular transformations, including the secondary structure loss, carboxylate group formation, and short peptide fragment generation, resulting in reduced structural order but enhanced thermal stability attributed to the stabilizing effect of sodium carboxylates

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