Published in

American Society for Microbiology, Applied and Environmental Microbiology, 6(59), p. 1774-1778, 1993

DOI: 10.1128/aem.59.6.1774-1778.1993

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Characterization of a nitrophenol reductase from the phototrophic bacterium Rhodobacter capsulatus E1F1.

Journal article published in 1993 by Rafael Blasco ORCID, Francisco Castillo
This paper is available in a repository.
This paper is available in a repository.

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Abstract

The phototrophic bacterium Rhodobacter capsulatus E1F1 photoreduced 2,4-dinitrophenol to 2-amino-4-nitrophenol by a nitrophenol reductase activity which was induced in the presence of nitrophenols and was repressed in ammonium-grown cells. The enzyme was located in the cytosol, required NAD(P)H as an electron donor, and used several nitrophenol derivatives as alternative substrates. The nitrophenol reductase was purified to electrophoretic homogeneity by a simple method. The enzyme was composed of two 27-kDa subunits, was inhibited by metal chelators, mercurial compounds, and Cu2+, and contained flavin mononucleotide and possibly nonheme iron as prosthetic groups. Purified enzyme also exhibited NAD(P)H diaphorase activity which used tetrazolium salt as an electron acceptor.