The influence of the proton concentration (pH 6.8, 7.4, 8.0) on the structure of the protein part of oxyhemoglobin was investigated in the work. Raman scattering showed that the transition to the oxidized state stabilizes the structure of the porphyrin ring, under these conditions the pH of the incubation environ does not affect the conformation of hemoporphyrin and its ability to transfer oxygen. A decrease in the ζ-potential of hemoglobin molecules was observed with increasing pH of the incubation environ, while the size of the molecule remains unchanged. An increase in the intensity and lifetime of fluorescence of tryptophan residues with an increase in the pH of the environ has been revealed, which indicates the presence of local conformational rearrangements that cause a change in the microenvironment of tryptophan in the protein part of hemoglobin. In this regard, in this paper, the relationship between the protein part and hemoporphyrin of human oxyhemoglobin in the pH of the incubation environ.
hemoglobin, pH, Raman scattering, ζ-potential, tryptophan fluorescence, hemoporphyrin, Bohr effect
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