Enhanced metabolism of 2,3',4,4',5-pentachlorobiphenyl (CB118) by bacterial cytochrome P450 monooxygenase mutants of Bacillus megaterium
Copyright © 2023 Elsevier B.V. All rights reserved..
Bacterial cytochrome P450 monooxygenase P450BM3 is a promising enzyme to provide novel substrate specificity and enhanced enzymatic activity. The wild type (WT) has been shown to metabolize the widely distributed polychlorinated biphenyl (PCB) 2,3',4,4',5-pentachlorobiphenyl (CB118) to hydroxylated metabolites. However, this reaction requires the coexistence of perfluoroalkyl carboxylic acids (PFCAs). To locate P450BM3 mutants metabolizing CB118 without PFCAs, mutations were selected from amino acids comprising the substrate-binding cavity and the substrate entrance. The mutant A264G showed enhanced hydroxylation activities compared to the WT for the production of five hydroxylated metabolites. Perfluorooctanoic acid addition provided the highest activity, as found in the WT. The docking model of A264G and CB118 indicated that the enlargement of the space above the heme brought CB118 close to the heme, resulting in high activity. In contrast, the mutants L188Q, QG, LVQ, and GVQ, which contain the L188Q mutation, showed higher activity than WT even without PFCAs. Docking models revealed that the closed form found in substrate binding was induced by the L188Q mutation in the substrate non-binding state of the mutants. These mutants are promising for bioremediation of PCBs using enhanced metabolizing activities.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:890 |
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| Enthalten in: |
The Science of the total environment - 890(2023) vom: 10. Sept., Seite 164475 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Ishida, Yuko [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 19.06.2023 Date Revised 19.06.2023 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.scitotenv.2023.164475 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM357597478 |
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| 100 | 1 | |a Ishida, Yuko |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Enhanced metabolism of 2,3',4,4',5-pentachlorobiphenyl (CB118) by bacterial cytochrome P450 monooxygenase mutants of Bacillus megaterium |
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| 500 | |a Date Completed 19.06.2023 | ||
| 500 | |a Date Revised 19.06.2023 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2023 Elsevier B.V. All rights reserved. | ||
| 520 | |a Bacterial cytochrome P450 monooxygenase P450BM3 is a promising enzyme to provide novel substrate specificity and enhanced enzymatic activity. The wild type (WT) has been shown to metabolize the widely distributed polychlorinated biphenyl (PCB) 2,3',4,4',5-pentachlorobiphenyl (CB118) to hydroxylated metabolites. However, this reaction requires the coexistence of perfluoroalkyl carboxylic acids (PFCAs). To locate P450BM3 mutants metabolizing CB118 without PFCAs, mutations were selected from amino acids comprising the substrate-binding cavity and the substrate entrance. The mutant A264G showed enhanced hydroxylation activities compared to the WT for the production of five hydroxylated metabolites. Perfluorooctanoic acid addition provided the highest activity, as found in the WT. The docking model of A264G and CB118 indicated that the enlargement of the space above the heme brought CB118 close to the heme, resulting in high activity. In contrast, the mutants L188Q, QG, LVQ, and GVQ, which contain the L188Q mutation, showed higher activity than WT even without PFCAs. Docking models revealed that the closed form found in substrate binding was induced by the L188Q mutation in the substrate non-binding state of the mutants. These mutants are promising for bioremediation of PCBs using enhanced metabolizing activities | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Docking model | |
| 650 | 4 | |a Hydroxylation | |
| 650 | 4 | |a Mutation | |
| 650 | 4 | |a P450BM3 | |
| 650 | 4 | |a Perfluoroalkyl carboxylic acid | |
| 650 | 4 | |a Polychlorinated biphenyl | |
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| 650 | 7 | |a Bacterial Proteins |2 NLM | |
| 700 | 1 | |a Goto, Erika |e verfasserin |4 aut | |
| 700 | 1 | |a Haga, Yuki |e verfasserin |4 aut | |
| 700 | 1 | |a Kubo, Makoto |e verfasserin |4 aut | |
| 700 | 1 | |a Itoh, Toshimasa |e verfasserin |4 aut | |
| 700 | 1 | |a Kasai, Chie |e verfasserin |4 aut | |
| 700 | 1 | |a Tsuzuki, Harunobu |e verfasserin |4 aut | |
| 700 | 1 | |a Nakamura, Miyune |e verfasserin |4 aut | |
| 700 | 1 | |a Shoji, Osami |e verfasserin |4 aut | |
| 700 | 1 | |a Yamamoto, Keiko |e verfasserin |4 aut | |
| 700 | 1 | |a Matsumura, Chisato |e verfasserin |4 aut | |
| 700 | 1 | |a Nakano, Takeshi |e verfasserin |4 aut | |
| 700 | 1 | |a Inui, Hideyuki |e verfasserin |4 aut | |
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