Bohr effect and oxygen affinity of carp, eel and human hemoglobin: Quantitative analyses provide rationale for the...

The functional properties of most fish hemoglobins are more complex than those of human hemoglobin. This complexity arises in the form of the Root effect, in which the oxygen affinity of such fish hemoglobins decreases rapidly with pH relative to that of human hemoglobin. Cooperative ligand binding is also diminished below pH ≈ 6.5. The Bohr effect, determined by acid-base titration, has been reported for the Root effect carp and anodic eel hemoglobins. Unlike for mammalian hemoglobins, the Wyman equation for the Bohr effect fails to account quantitatively for these Bohr data. We present a successful quantitative accounting for these data based on evidence for multiple T states in various fish hemoglobins and on their lack of sixhistidine Bohr groups, with pK^oxy > pK^deoxy. On the same bases we also provide a rationale for the higher pH sensitivity of the oxygen affinity of carp compared to human hemoglobin.