Reduction of Peroxides and Dinitrobenzenes byMycobacterium tuberculosisThioredoxin and Thioredoxin Reductase
| Autor: | Zhoupeng Zhang, Patrick J. Hillas, Paul R. Ortiz de Montellano |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Thioredoxin-Disulfide Reductase
animal structures Antioxidant Free Radicals medicine.medical_treatment Thioredoxin reductase Biophysics medicine.disease_cause Biochemistry Mycobacterium tuberculosis chemistry.chemical_compound Thioredoxins tert-Butylhydroperoxide Benzene Derivatives medicine Molecular Biology Escherichia coli Chromatography High Pressure Liquid chemistry.chemical_classification Oxidase test biology Hydrogen Peroxide Oxidants biology.organism_classification Peroxides Dinitrobenzenes Oxidative Stress Enzyme chemistry Cumene hydroperoxide Thioredoxin Oxidation-Reduction |
| Zdroj: | Archives of Biochemistry and Biophysics. 363:19-26 |
| ISSN: | 0003-9861 |
| DOI: | 10.1006/abbi.1998.1056 |
| Popis: | The thioredoxin (Trx) and thioredoxin reductase (TR) of Mycobacterium tuberculosis have been expressed in Escherichia coli and shown to reduce peroxides and dinitrobenzenes. The reduction of H 2 O 2 requires both Trx and TR and is more efficient under anaerobic than aerobic conditions. In contrast, cumene hydroperoxide is reduced to cumyl alcohol and acetophenone in a process that requires NADPH and TR but not Trx. Cumene hydroperoxide reduction is partially inhibited by chelation of trace metals in the medium. The reduction of cumene hydroperoxide by TR is more effective under anaerobic than aerobic conditions due to a competing oxidase reaction in which electrons are transferred from TR to O 2 . Under anaerobic conditions, dinitrobenzenes also serve as electron acceptors and are reduced by TR to nitroanilines, but the enzyme does not reduce mononitrobenzenes or mononitroimidazoles such as metronidazole. The reductive activity of the Trx–TR system may modify the antioxidant defenses of M. tuberculosis. |
| Databáze: | OpenAIRE |
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