Histidine residues of myoglobin studied by 1H nuclear magnetic resonance spectroscopy
Abstract
Titration curves of all the H-2 and H-4 resonances of the eleven titrating histidine residues in ferrous carbon monoxide sperm whale myoglobin are given; the H-4 resonance of the distal histidine has been observed at ca. 2·2 p.p.m. upfield of its normal position and on titration, the distal histidine resonances give a pK′ of 5·2 at 40 °C.
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