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Substitution of the heme binding module in hemoglobin alpha- and beta-subunits. Implication for different regulation mechanisms of the heme proximal structure between hemoglobin and myoglobin.
Inaba K, Ishimori K, Imai K, Morishima I. Inaba K, et al. Among authors: ishimori k. J Biol Chem. 2000 Apr 28;275(17):12438-45. doi: 10.1074/jbc.275.17.12438. J Biol Chem. 2000. PMID: 10777528 Free article.
In our previous work, we demonstrated that the replacement of the "heme binding module," a segment from F1 to G5 site, in myoglobin with that of hemoglobin alpha-subunit converted the heme proximal structure of myoglobin into the alpha-subunit type (Inaba, K., Ishimori
In our previous work, we demonstrated that the replacement of the "heme binding module," a segment from F1 to G5 site, in myoglobin with tha …
181 results