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Unexpected role of electron-transfer hub in direct degradation of pollutants by exoelectrogenic bacteria.
Zhu, Ting-Ting; Cheng, Zhou-Hua; Yu, Sheng-Song; Li, Wen-Wei; Liu, Dong-Feng; Yu, Han-Qing.
Afiliación
  • Zhu TT; CAS Key Laboratory of Urban Pollutant Conversion, Department of Environmental Science and Engineering, University of Science and Technology of China, Hefei, 230026, China.
  • Cheng ZH; School of Life Sciences, University of Science and Technology of China, Hefei, 230026, China.
  • Yu SS; CAS Key Laboratory of Urban Pollutant Conversion, Department of Environmental Science and Engineering, University of Science and Technology of China, Hefei, 230026, China.
  • Li WW; CAS Key Laboratory of Urban Pollutant Conversion, Department of Environmental Science and Engineering, University of Science and Technology of China, Hefei, 230026, China.
  • Liu DF; University of Science and Technology of China-City University of Hong Kong Joint Advanced Research Center, Suzhou Institute for Advanced Research of USTC, Suzhou, 215123, China.
  • Yu HQ; CAS Key Laboratory of Urban Pollutant Conversion, Department of Environmental Science and Engineering, University of Science and Technology of China, Hefei, 230026, China.
Environ Microbiol ; 24(4): 1838-1848, 2022 04.
Article en En | MEDLINE | ID: mdl-35170205
Exoelectrogenic bacteria (EEB) are capable of anaerobic respiration with diverse extracellular electron acceptors including insoluble minerals, electrodes and flavins, but the detailed electron transfer pathways and reaction mechanisms remain elusive. Here, we discover that CymA, which is usually considered to solely serve as an inner-membrane electron transfer hub in Shewanella oneidensis MR-1 (a model EEB), might also function as a reductase for direct reducing diverse nitroaromatic compounds (e.g. 2,4-dichloronitrobenzene) and azo dyes. Such a process can be accelerated by dosing anthraquinone-2,6-disulfonate. The CymA-based reduction pathways in S. oneidensis MR-1 for different contaminants could be functionally reconstructed and strengthened in Escherichia coli. The direct reduction of lowly polar contaminants by quinol oxidases like CymA homologues might be universal in diverse microbes. This work offers new insights into the pollutant reduction mechanisms of EEB and unveils a new function of CymA to act as a terminal reductase.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Shewanella / Contaminantes Ambientales Idioma: En Revista: Environ Microbiol Asunto de la revista: MICROBIOLOGIA / SAUDE AMBIENTAL Año: 2022 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Shewanella / Contaminantes Ambientales Idioma: En Revista: Environ Microbiol Asunto de la revista: MICROBIOLOGIA / SAUDE AMBIENTAL Año: 2022 Tipo del documento: Article País de afiliación: China