A method has been developed for the sol–gel encapsulation of hemoglobin in the deoxygenated T-conformation followed by saturation of the protein with molecular oxygen (O2). A device for the sol–gel encapsulation of hemoglobin under anaerobic conditions has been constructed. Kinetic data for the bimolecular recombination of O2 with encapsulated hemoglobin stabilized predominantly in the oxygenated T-conformation (in an ensemble of oxygenated T-conformers were measured for the first time using time-resolved absorption spectroscopy. This method permits detailed study of the O2-binding properties of the nonequilibrium conformational states of hemoglobin, which significantly contributes to our understanding of the mechanism of the regulation of O2 binding by both native human hemoglobin and artificial oxygen carriers.
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Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 90, No. 2, pp. 165–173, March–April, 2023. https://doi.org/10.47612/051475062023902165173.
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Lepeshkevich, S.V., Parkhats, M.V. & Dzhagarov, B.M. Bimolecular Recombination of Molecular Oxygen with Sol–Gel Encapsulated Hemoglobin in a Nonequilibrium T-Conformation. J Appl Spectrosc 90, 265–273 (2023). https://doi.org/10.1007/s10812-023-01531-9
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DOI: https://doi.org/10.1007/s10812-023-01531-9