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Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation
Hemoglobin is the main protein of red blood cells that provides oxygen transport to all cells of the human body. The ability of hemoglobin to bind the main low-molecular-weight thiol of the cell glutathione, both covalently and noncovalently, is not only an important part of the antioxidant protecti...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10487563/ https://www.ncbi.nlm.nih.gov/pubmed/37686361 http://dx.doi.org/10.3390/ijms241713557 |
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author | Kuleshova, Iuliia D. Zaripov, Pavel I. Poluektov, Yuri M. Anashkina, Anastasia A. Kaluzhny, Dmitry N. Parshina, Evgeniia Yu. Maksimov, Georgy V. Mitkevich, Vladimir A. Makarov, Alexander A. Petrushanko, Irina Yu. |
author_facet | Kuleshova, Iuliia D. Zaripov, Pavel I. Poluektov, Yuri M. Anashkina, Anastasia A. Kaluzhny, Dmitry N. Parshina, Evgeniia Yu. Maksimov, Georgy V. Mitkevich, Vladimir A. Makarov, Alexander A. Petrushanko, Irina Yu. |
author_sort | Kuleshova, Iuliia D. |
collection | PubMed |
description | Hemoglobin is the main protein of red blood cells that provides oxygen transport to all cells of the human body. The ability of hemoglobin to bind the main low-molecular-weight thiol of the cell glutathione, both covalently and noncovalently, is not only an important part of the antioxidant protection of red blood cells, but also affects its affinity for oxygen in both cases. In this study, the properties of oxyhemoglobin in complex with reduced glutathione (GSH) and properties of glutathionylated hemoglobin bound to glutathione via an SS bond were characterized. For this purpose, the methods of circular dichroism, Raman spectroscopy, infrared spectroscopy, tryptophan fluorescence, differential scanning fluorimetry, and molecular modeling were used. It was found that the glutathionylation of oxyhemoglobin caused changes in the secondary structure of the protein, reducing the alpha helicity, but did not affect the heme environment, tryptophan fluorescence, and the thermostability of the protein. In the noncovalent complex of oxyhemoglobin with reduced glutathione, the secondary structure of hemoglobin remained almost unchanged; however, changes in the heme environment and the microenvironment of tryptophans, as well as a decrease in the protein’s thermal stability, were observed. Thus, the formation of a noncovalent complex of hemoglobin with glutathione makes a more significant effect on the tertiary and quaternary structure of hemoglobin than glutathionylation, which mainly affects the secondary structure of the protein. The obtained data are important for understanding the functioning of glutathionylated hemoglobin, which is a marker of oxidative stress, and hemoglobin in complex with GSH, which appears to deposit GSH and release it during deoxygenation to increase the antioxidant protection of cells. |
format | Online Article Text |
id | pubmed-10487563 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-104875632023-09-09 Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation Kuleshova, Iuliia D. Zaripov, Pavel I. Poluektov, Yuri M. Anashkina, Anastasia A. Kaluzhny, Dmitry N. Parshina, Evgeniia Yu. Maksimov, Georgy V. Mitkevich, Vladimir A. Makarov, Alexander A. Petrushanko, Irina Yu. Int J Mol Sci Article Hemoglobin is the main protein of red blood cells that provides oxygen transport to all cells of the human body. The ability of hemoglobin to bind the main low-molecular-weight thiol of the cell glutathione, both covalently and noncovalently, is not only an important part of the antioxidant protection of red blood cells, but also affects its affinity for oxygen in both cases. In this study, the properties of oxyhemoglobin in complex with reduced glutathione (GSH) and properties of glutathionylated hemoglobin bound to glutathione via an SS bond were characterized. For this purpose, the methods of circular dichroism, Raman spectroscopy, infrared spectroscopy, tryptophan fluorescence, differential scanning fluorimetry, and molecular modeling were used. It was found that the glutathionylation of oxyhemoglobin caused changes in the secondary structure of the protein, reducing the alpha helicity, but did not affect the heme environment, tryptophan fluorescence, and the thermostability of the protein. In the noncovalent complex of oxyhemoglobin with reduced glutathione, the secondary structure of hemoglobin remained almost unchanged; however, changes in the heme environment and the microenvironment of tryptophans, as well as a decrease in the protein’s thermal stability, were observed. Thus, the formation of a noncovalent complex of hemoglobin with glutathione makes a more significant effect on the tertiary and quaternary structure of hemoglobin than glutathionylation, which mainly affects the secondary structure of the protein. The obtained data are important for understanding the functioning of glutathionylated hemoglobin, which is a marker of oxidative stress, and hemoglobin in complex with GSH, which appears to deposit GSH and release it during deoxygenation to increase the antioxidant protection of cells. MDPI 2023-08-31 /pmc/articles/PMC10487563/ /pubmed/37686361 http://dx.doi.org/10.3390/ijms241713557 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kuleshova, Iuliia D. Zaripov, Pavel I. Poluektov, Yuri M. Anashkina, Anastasia A. Kaluzhny, Dmitry N. Parshina, Evgeniia Yu. Maksimov, Georgy V. Mitkevich, Vladimir A. Makarov, Alexander A. Petrushanko, Irina Yu. Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation |
title | Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation |
title_full | Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation |
title_fullStr | Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation |
title_full_unstemmed | Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation |
title_short | Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation |
title_sort | changes in hemoglobin properties in complex with glutathione and after glutathionylation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10487563/ https://www.ncbi.nlm.nih.gov/pubmed/37686361 http://dx.doi.org/10.3390/ijms241713557 |
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