Bimolecular Recombination of Molecular Oxygen with Sol–Gel Encapsulated Hemoglobin in a Nonequilibrium T-Conformation

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 (O 2 ). A device for the sol–gel encapsulation of hemoglobin under anaerobic conditions has been constructed. Kinetic data for the b...

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Bibliographic Details
Published in:Journal of applied spectroscopy 2023-05, Vol.90 (2), p.265-273
Main Authors: Lepeshkevich, S. V., Parkhats, M. V., Dzhagarov, B. M.
Format: Article
Language:English
Subjects:
Absorption spectroscopy
Anaerobic conditions
Analytical Chemistry
Atomic/Molecular Structure and Spectra
Binding
Deoxygenation
Encapsulation
Glycosylated hemoglobin
Hemoglobin
Oxygen
Oxygenation
Physics
Physics and Astronomy
Sol-gel processes
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Summary: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 (O 2 ). A device for the sol–gel encapsulation of hemoglobin under anaerobic conditions has been constructed. Kinetic data for the bimolecular recombination of O 2 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 O 2 -binding properties of the nonequilibrium conformational states of hemoglobin, which significantly contributes to our understanding of the mechanism of the regulation of O 2 binding by both native human hemoglobin and artificial oxygen carriers.
ISSN:0021-9037
1573-8647
DOI:10.1007/s10812-023-01531-9