Abstract
A 220 MHz proton magnetic resonance study of the downfield (7 to 9 p.p.m.) region of two metmyoglobins as a function of pH reveals seven titrating histidine C(2) protons in sperm whale and six in horse heart myoglobin. Comparison between the results for these two proteins and the use of computer curve-fitting facilitates the determination of the continuities of the titration curves and the apparent ionization constants. One titration curve in each case is shifted upfield relative to the other curves and has a much higher p K a value (8·05 in sperm whale metmyoglobin). Possible assignments of the resonances are discussed from the consideration of the environments of the histidine residues in the X-ray structure of sperm whale myoglobin.
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