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• W2014972072 abstract "Abstract The cobalt(II) derivative of human serum transferrin has been prepared and investigated through electronic and 1 H NMR spectroscopy. Cobalt(II) binds the protein quantitatively in a 2:1 ratio; metal binding requires invariantly the presence of the synergistic anion and occurs at the same binding sites as iron(III). Intersite differences are very slight; on the other hand, there are marked differences in the absorption and CD spectra of Co(II) 2 Tf with respect to Co(II) 2 OTf which could be explained on the ground of differences in the coordination polyhedron and in the chirality. 1 H NMR spectroscopy of the cobalt(II) derivatives allows selective detection of the isotropically shifted signals from protons of the metal coordinated residues and can be used at a first stage as an extremely sensitive conformational fingerprint." @default.
• W2014972072 created "2016-06-24" @default.
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• W2014972072 date "1990-08-01" @default.
• W2014972072 modified "2023-09-27" @default.
• W2014972072 title "Cobalt(II) as a probe of the metal binding sites of transferrins" @default.
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• W2014972072 doi "https://doi.org/10.1016/s0020-1693(00)80288-1" @default.
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