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The following asymmetric alpha 1 99 Lys-alpha 2 99 Lys cross-linked Fe(II)-Co(II) hybrid hemoglobins (Hbs) were first prepared from derivatives of hemoglobin C (beta 6 Glu-Lys) and human normal HbA: [alpha(Co)beta(Fe)]A[alpha(Co)beta(Co)]cXL, [alpha(Fe)beta(Co)]A[alpha(Co)beta(Co)]cXL, etc. Their 500 MHz 1H NMR and EPR spectra were measured in order to study the change in their tertiary and quaternary structure under atmosphere of deoxy, oxy and carbon monoxide (with or without IHP). From the change of T and R marks in 1H NMR hydrogen bonding region, it is proved that oxygen molecules are first bonded to alpha(Fe) subunits rather than to beta(Fe). The experimental phenomena provided further evidence that intermediate states of ligation are present in addition to T and R state during process of binding of oxygen to Hb. IHP facilitates transformation of T state to R state. The same conclusion can also be drawn from the results of EPR spectra at 77 K.
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