Functional Nonequivalence of α and β Hemes in Human Adult Hemoglobin

Abstract

Nuclear magnetic resonance studies of the contact-shifted spectra of heme protons in deoxyhemoglobin A from human adults show conclusively that oxygen binds to the α hemes in preference to the β hemes. The preferential binding is produced in 10% hemoglobin solution at neutral pH by either a 15-fold molar excess of 2,3-diphosphoglycerate or a 5-fold molar excess of inositol hexaphosphate. Preferential binding is not observable in the absence of the organic phosphates. The results indicate that the oxygenation of hemoglobin may be described by a sequential model, or by a concerted model that allows the α hemes to bind ligand first.

• NMR
• preferential ligand binding
• organic phosphates
• models of cooperative ligand binding