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The formation of HbFe(II)NO in hypoxic RBCs pretreated with NO was measured by EPR. The signature three-peak hyperfine splitting demonstrated that NO was primarily bound to the α heme subunit under hypoxia and was primarily in the low-oxygen affinity T state (upper black line). On oxygenation, NO remained bound to the α heme subunit, whereas Hb converted to the high oxygen affinity R state (lower gray line).
