Solution of the spatial structure of dimeric transmembrane domains of proteins by heteronuclear NMR spectroscopy and molecular modeling |
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| Authors: | P E Volynsky E V Bocharov D E Nolde Ya A Vereschaga M L Mayzel K S Mineev E A Mineeva Yu E Pustovalova I A Gagnidze R G Efremov A S Arseniev |
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| Institution: | (1) Grodno State Medical University, ul. Gor’kogo 80, Grodno, 230015, Belarus |
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| Abstract: | The goal of the work was to asses the effect of peroxynitrite on the affinity of hemoglobin for oxygen in in vitro experiments. It was demonstrated that the incubation of whole venous blood with peroxynitrite increased the affinity of hemoglobin for oxygen. Presumably, this effect is realized through generation of various forms of hemoglobin: heme-oxidized and modified at amino acid residues of the protein. The dependence of the results of hemoglobin-peroxynitrite reactions on carbon dioxide tension and the degree of hemoglobin oxygenation is discussed. |
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| Keywords: | hemoglobin peroxynitrite affinity of hemoglobin for oxygen |
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