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Kinetic characterization of the acid—alkaline transition in Dolabella auricularia ferric myoglobin using 1 H‐NMR saturation transfer experiments
Author(s) -
Yamamoto Yasuhiko,
Chûjô Riichirô,
Inoue Yoshio,
Suzuki Tomohiko
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81149-g
Subject(s) - myoglobin , chemistry , heme , ferric , hemeprotein , proton nmr , metmyoglobin , kinetics , saturation (graph theory) , stereochemistry , inorganic chemistry , photochemistry , organic chemistry , enzyme , physics , mathematics , quantum mechanics , combinatorics
The acid—alkaline transition in ferric myoglobin of the mollusc, Dolabella auricularia , exerts the changes in both the coordination and spin states of the heme iron. Slower transition rate, compared to the NMR time scale, in this myoglobin allowed the observation of separate signals arising from the two forms, and pH tiltration yielded a p K value of 7.8. 1 H‐NMR saturation transfer experiments have been successfully used not only to provide the first signal assignments for the heme methyl proton resonances of the Met‐hydroxyl form of the myoglobin, but also to detemine the kinetics of the transition.