Carbon monoxide binding to hemoglobins from a of sources has been studied by ^(13)C nuclear magnetic . The two resonances have been specifically assigned ^(13)CO bound to α or to β subunits. The reason for the anomalous of ^(13)CO bound to the a chain of rabbit hemoglobin is discussed with particular reference to residue Phe-48 (CD6). relative facility with which oxygen displaces carbon monoxide, the relative thermodynamic affinity for carbon monoxide to the unliganded state, of the α and β subunits found to differ.
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Moon et al. (1974) studied this question.