NADH and NADPH peroxidases as antioxidant defense mechanisms in intestinal sulfate-reducing bacteria
Abstract Animal and human feces typically include intestinal sulfate-reducing bacteria (SRB). Hydrogen sulfide and acetate are the end products of their dissimilatory sulfate reduction and may create a synergistic effect. Here, we report NADH and NADPH peroxidase activities from intestinal SRB Desul...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-08-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-023-41185-3 |
| _version_ | 1797452823290445824 |
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| author | Ivan Kushkevych Dani Dordević Mohammad I. Alberfkani Márió Gajdács Eszter Ostorházi Monika Vítězová Simon K.-M. R. Rittmann |
| author_facet | Ivan Kushkevych Dani Dordević Mohammad I. Alberfkani Márió Gajdács Eszter Ostorházi Monika Vítězová Simon K.-M. R. Rittmann |
| author_sort | Ivan Kushkevych |
| collection | DOAJ |
| description | Abstract Animal and human feces typically include intestinal sulfate-reducing bacteria (SRB). Hydrogen sulfide and acetate are the end products of their dissimilatory sulfate reduction and may create a synergistic effect. Here, we report NADH and NADPH peroxidase activities from intestinal SRB Desulfomicrobium orale and Desulfovibrio piger. We sought to compare enzymatic activities under the influence of various temperature and pH regimes, as well as to carry out kinetic analyses of enzymatic reaction rates, maximum amounts of the reaction product, reaction times, maximum rates of the enzyme reactions, and Michaelis constants in cell-free extracts of intestinal SRB, D. piger Vib-7, and D. orale Rod-9, collected from exponential and stationary growth phases. The optimal temperature (35 °C) and pH (7.0) for both enzyme’s activity were determined. The difference in trends of Michaelis constants (K m) during exponential and stationary phases are noticeable between D. piger Vib-7 and D. orale Rod-9; D. orale Rod-9 showed much higher K m (the exception is NADH peroxidase of D. piger Vib-7: 1.42 ± 0.11 mM) during the both monitored phases. Studies of the NADH and NADPH peroxidases—as putative antioxidant defense systems of intestinal SRB and detailed data on the kinetic properties of this enzyme, as expressed by the decomposition of hydrogen peroxide—could be important for clarifying evolutionary mechanisms of antioxidant defense systems, their etiological role in the process of dissimilatory sulfate reduction, and their possible role in the development of bowel diseases. |
| first_indexed | 2024-03-09T15:14:14Z |
| format | Article |
| id | doaj.art-f78b6bbab5d24e7cbd727b309f6ef73a |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-03-09T15:14:14Z |
| publishDate | 2023-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-f78b6bbab5d24e7cbd727b309f6ef73a2023-11-26T13:13:21ZengNature PortfolioScientific Reports2045-23222023-08-0113111110.1038/s41598-023-41185-3NADH and NADPH peroxidases as antioxidant defense mechanisms in intestinal sulfate-reducing bacteriaIvan Kushkevych0Dani Dordević1Mohammad I. Alberfkani2Márió Gajdács3Eszter Ostorházi4Monika Vítězová5Simon K.-M. R. Rittmann6Department of Experimental Biology, Faculty of Science, Masaryk UniversityDepartment of Plant Origin Food Sciences, Faculty of Veterinary Hygiene and Ecology, University of Veterinary Sciences BrnoDepartment of Medical Laboratory Technology, College of Health and Medical Techniques, Duhok Polytechnic UniversityDepartment of Oral Biology and Experimental Dental Research, Faculty of Dentistry, University of SzegedFaculty of Medicine, Institute of Medical Microbiology, Semmelweis UniversityDepartment of Experimental Biology, Faculty of Science, Masaryk UniversityArchaea Physiology & Biotechnology Group, Department of Functional and Evolutionary Ecology, Universität WienAbstract Animal and human feces typically include intestinal sulfate-reducing bacteria (SRB). Hydrogen sulfide and acetate are the end products of their dissimilatory sulfate reduction and may create a synergistic effect. Here, we report NADH and NADPH peroxidase activities from intestinal SRB Desulfomicrobium orale and Desulfovibrio piger. We sought to compare enzymatic activities under the influence of various temperature and pH regimes, as well as to carry out kinetic analyses of enzymatic reaction rates, maximum amounts of the reaction product, reaction times, maximum rates of the enzyme reactions, and Michaelis constants in cell-free extracts of intestinal SRB, D. piger Vib-7, and D. orale Rod-9, collected from exponential and stationary growth phases. The optimal temperature (35 °C) and pH (7.0) for both enzyme’s activity were determined. The difference in trends of Michaelis constants (K m) during exponential and stationary phases are noticeable between D. piger Vib-7 and D. orale Rod-9; D. orale Rod-9 showed much higher K m (the exception is NADH peroxidase of D. piger Vib-7: 1.42 ± 0.11 mM) during the both monitored phases. Studies of the NADH and NADPH peroxidases—as putative antioxidant defense systems of intestinal SRB and detailed data on the kinetic properties of this enzyme, as expressed by the decomposition of hydrogen peroxide—could be important for clarifying evolutionary mechanisms of antioxidant defense systems, their etiological role in the process of dissimilatory sulfate reduction, and their possible role in the development of bowel diseases.https://doi.org/10.1038/s41598-023-41185-3 |
| spellingShingle | Ivan Kushkevych Dani Dordević Mohammad I. Alberfkani Márió Gajdács Eszter Ostorházi Monika Vítězová Simon K.-M. R. Rittmann NADH and NADPH peroxidases as antioxidant defense mechanisms in intestinal sulfate-reducing bacteria Scientific Reports |
| title | NADH and NADPH peroxidases as antioxidant defense mechanisms in intestinal sulfate-reducing bacteria |
| title_full | NADH and NADPH peroxidases as antioxidant defense mechanisms in intestinal sulfate-reducing bacteria |
| title_fullStr | NADH and NADPH peroxidases as antioxidant defense mechanisms in intestinal sulfate-reducing bacteria |
| title_full_unstemmed | NADH and NADPH peroxidases as antioxidant defense mechanisms in intestinal sulfate-reducing bacteria |
| title_short | NADH and NADPH peroxidases as antioxidant defense mechanisms in intestinal sulfate-reducing bacteria |
| title_sort | nadh and nadph peroxidases as antioxidant defense mechanisms in intestinal sulfate reducing bacteria |
| url | https://doi.org/10.1038/s41598-023-41185-3 |
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