Identification of the titrating group in the heme cavity of myoglobin. Evidence for the heme-protein pi-pi interaction.
The pH dependence of the proton NMR chemical shifts of met-cyano and deoxy forms of native and reconstituted myoglobins reflects a structural transition in the heme pocket modulated by a single proton with pK 5.1-5.6. Comparison of this pH dependence of sperm whale and elephant myoglobin and that of the former protein reconstituted with esterified hemin eliminates both the distal histidine as well as the heme propionates as the titrating residue. Reconstitution of sperm whale met-cyano myoglobin with hemin modified at the 2,4-positions leads to a systematic variation in the pK for the structural transition, thus indicating the presence of a coupling between the titrating group and the heme pi system. The results are consistent with histidine FG3 (His-FG3) being the titrating group, and a donor-acceptor pi-pi interaction between its imidazole and the heme is proposed.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D004606:Elephants; D006420:Hemeproteins; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D009211:Myoglobin; D013045:Species Specificity; D014907:Whales
D006420:Hemeproteins; D009211:Myoglobin