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Expressed Soybean Leghemoglobin: Effect on Escherichia coli at Oxidative and Nitrosative Stress
Leghemoglobin (Lb) is an oxygen-binding plant hemoglobin of legume nodules, which participates in the symbiotic nitrogen fixation process. Another way to obtain Lb is its expression in bacteria, yeasts, or other organisms. This is promising for both obtaining Lb in the necessary quantity and scrutin...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8659191/ https://www.ncbi.nlm.nih.gov/pubmed/34885789 http://dx.doi.org/10.3390/molecules26237207 |
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author | Kosmachevskaya, Olga V. Nasybullina, Elvira I. Shumaev, Konstantin B. Topunov, Alexey F. |
author_facet | Kosmachevskaya, Olga V. Nasybullina, Elvira I. Shumaev, Konstantin B. Topunov, Alexey F. |
author_sort | Kosmachevskaya, Olga V. |
collection | PubMed |
description | Leghemoglobin (Lb) is an oxygen-binding plant hemoglobin of legume nodules, which participates in the symbiotic nitrogen fixation process. Another way to obtain Lb is its expression in bacteria, yeasts, or other organisms. This is promising for both obtaining Lb in the necessary quantity and scrutinizing it in model systems, e.g., its interaction with reactive oxygen (ROS) and nitrogen (RNS) species. The main goal of the work was to study how Lb expression affected the ability of Escherichia coli cells to tolerate oxidative and nitrosative stress. The bacterium E. coli with the embedded gene of soybean leghemoglobin a contains this protein in an active oxygenated state. The interaction of the expressed Lb with oxidative and nitrosative stress inducers (nitrosoglutathione, tert-butyl hydroperoxide, and benzylviologen) was studied by enzymatic methods and spectrophotometry. Lb formed NO complexes with heme-nitrosylLb or nonheme iron-dinitrosyl iron complexes (DNICs). The formation of Lb-bound DNICs was also detected by low-temperature electron paramagnetic resonance spectroscopy. Lb displayed peroxidase activity and catalyzed the reduction of organic peroxides. Despite this, E. coli-synthesized Lb were more sensitive to stress inducers. This might be due to the energy demand required by the Lb synthesis, as an alien protein consumes bacterial resources and thereby decreases adaptive potential of E. coli. |
format | Online Article Text |
id | pubmed-8659191 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-86591912021-12-10 Expressed Soybean Leghemoglobin: Effect on Escherichia coli at Oxidative and Nitrosative Stress Kosmachevskaya, Olga V. Nasybullina, Elvira I. Shumaev, Konstantin B. Topunov, Alexey F. Molecules Article Leghemoglobin (Lb) is an oxygen-binding plant hemoglobin of legume nodules, which participates in the symbiotic nitrogen fixation process. Another way to obtain Lb is its expression in bacteria, yeasts, or other organisms. This is promising for both obtaining Lb in the necessary quantity and scrutinizing it in model systems, e.g., its interaction with reactive oxygen (ROS) and nitrogen (RNS) species. The main goal of the work was to study how Lb expression affected the ability of Escherichia coli cells to tolerate oxidative and nitrosative stress. The bacterium E. coli with the embedded gene of soybean leghemoglobin a contains this protein in an active oxygenated state. The interaction of the expressed Lb with oxidative and nitrosative stress inducers (nitrosoglutathione, tert-butyl hydroperoxide, and benzylviologen) was studied by enzymatic methods and spectrophotometry. Lb formed NO complexes with heme-nitrosylLb or nonheme iron-dinitrosyl iron complexes (DNICs). The formation of Lb-bound DNICs was also detected by low-temperature electron paramagnetic resonance spectroscopy. Lb displayed peroxidase activity and catalyzed the reduction of organic peroxides. Despite this, E. coli-synthesized Lb were more sensitive to stress inducers. This might be due to the energy demand required by the Lb synthesis, as an alien protein consumes bacterial resources and thereby decreases adaptive potential of E. coli. MDPI 2021-11-28 /pmc/articles/PMC8659191/ /pubmed/34885789 http://dx.doi.org/10.3390/molecules26237207 Text en © 2021 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 Kosmachevskaya, Olga V. Nasybullina, Elvira I. Shumaev, Konstantin B. Topunov, Alexey F. Expressed Soybean Leghemoglobin: Effect on Escherichia coli at Oxidative and Nitrosative Stress |
title | Expressed Soybean Leghemoglobin: Effect on Escherichia coli at Oxidative and Nitrosative Stress |
title_full | Expressed Soybean Leghemoglobin: Effect on Escherichia coli at Oxidative and Nitrosative Stress |
title_fullStr | Expressed Soybean Leghemoglobin: Effect on Escherichia coli at Oxidative and Nitrosative Stress |
title_full_unstemmed | Expressed Soybean Leghemoglobin: Effect on Escherichia coli at Oxidative and Nitrosative Stress |
title_short | Expressed Soybean Leghemoglobin: Effect on Escherichia coli at Oxidative and Nitrosative Stress |
title_sort | expressed soybean leghemoglobin: effect on escherichia coli at oxidative and nitrosative stress |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8659191/ https://www.ncbi.nlm.nih.gov/pubmed/34885789 http://dx.doi.org/10.3390/molecules26237207 |
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