Abstract
Two-dimensional 1H nuclear magnetic resonance exchange spectroscopy has been applied to the study of the pyridine-ligated complex of equine metmyoglobin (Py-metMb). With the known resonance assignment of metMb, some hyperfine shifted resonances of the Py-metMb complex have been assigned for the first time. Based on a matrix formalism, the kinetic and equilibrium data for pyridine binding to metMb have been evaluated from the 2D peak amplitudes. A qualitative comparison of the methyl shift pattern in metMbCN −, metMbN 3 − and imidazole metMb (metMbIm) with Py-metMb shows a reverse methyl shift between pyrrole I and IV, and the reason for this is discussed.
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