Dehydrogenation, oxidative denitration and ring contraction of N,N-dinnethyl-5-nitrouracil by a Bacillus nitroreductase Nfr-A1
| Autor: | Sylvie Cortial, Sophie Dezard, Philippe Chaignon, Didier Sergent, Jamal Ouazzani |
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| Přispěvatelé: | Institut de Chimie des Substances Naturelles (ICSN), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC) |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Double bond Stereochemistry [CHIM.ORGA]Chemical Sciences/Organic chemistry Process Chemistry and Technology Bioengineering Flavin group Oxidative phosphorylation Biochemistry Catalysis 03 medical and health sciences chemistry.chemical_compound Nitroreductase 0302 clinical medicine chemistry 030220 oncology & carcinogenesis Nitro Dehydrogenation Hydrogen peroxide ComputingMilieux_MISCELLANEOUS 030304 developmental biology |
| Zdroj: | Journal of Molecular Catalysis B: Enzymatic Journal of Molecular Catalysis B: Enzymatic, Elsevier, 2012, 76, pp.761-768. ⟨10.1016/j.molcatb.2011.11.014⟩ |
| ISSN: | 1381-1177 |
| Popis: | Nfr-A1, a Bacillus subtilis nitroreductase, catalyzes the nitroreduction of a large panel of aromatic and heterocyclic nitro compounds, except those belonging to nitrouracil class of molecules. Besides nitroreduction, Nfr-A1 exhibits a strong NADH oxidase activity in the presence of oxygen, leading to high concentration of H 2 O 2 (up to 200 μM). In the presence of ( N , N )-dimethyl-5-nitrouracil 1 (dim-NU), Nfr-A1 achieves the reduction of dim-NU double bond to compounds 2 and 3 and in parallel the oxidation of dim-NU to the denitrated five membered derivatives 4 and 5 . The reduction is catalyzed by the reduced flavin Fl- Red and resembles those catalyzed by dihydropyrimidine dehydrogenases (DPD), during the catabolism of pyrimidines. The oxidative denitration is catalyzed in part by hydrogen peroxide generated through the NADH-oxidase activity, and certainly by the peroxyflavin intermediate Fl- OOH for the other part. The mechanisms of reaction were proposed according to experimental data and literature. These findings together with our previous results on the potential biological role of Nfr-A1, confirm the large spectrum of catalysis supported by this enzyme. The oxidative denitration is sporadically reported in literature and represents a safe and green alternative for the remediation of nitro-compounds. |
| Databáze: | OpenAIRE |
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