European Journal of Biochemistry · 1969 · 39 citations · 11 references
Distal HistidineFunctional PropertiesMolecular BiologyChemical BiologyRedox BiologyOxidative StressHematologyHemoglobin ZürichBiochemistryHeme SignalingHeme TransportHeme HomeostasisPeriodic Surface StructuresNatural SciencesPhysiologyBohr Effect ProtonsMetabolismMedicineChemical Kinetics
Hemoglobin Zürich (β 63 His → Arg ) has a higher affinity for oxygen and for ethyl isocyanide than hemoglobin A. It shows a decreased value of n in the Hill equation (∼ 1.8 for O 2 and 1.0 for ethyl isocyanide). However, the Bohr effect is normal, thus excluding the distal histidine as the donor of the Bohr effect protons. The kinetics of combination with CO differs largely from that of hemoglobin A.
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