Affiliation:
1. Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Córdoba, Spain.
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.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Reference32 articles.
1. Light-dependent degradation of nitrophenols by the phototrophic bacterium Rhodobacter capsulatus ElFl;Blasco R.;Appl. Environ. Microbiol.,1992
2. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding;Bradford M. M.;Anal. Biochem.,1976
3. Brewer J. M. A. J. Pesce and T. E. Spencer. 1974. Ultracentrifugation p. 161-215. In J. M. Brewer A. J. Pesce and R. B. Ashworth (ed.) Experimental techniques in biochemistry. Prentice-Hall Englewood Cliffs N.J.
4. Bacterial degradation of the nitrobenzoic acids. II. Reduction of the nitro group;Cartwright N. J.;Biochem. J.,1959
5. Nitrate reduction by photosynthetic purple bacteria;Castillo F.;Photosynth. Res.,1982
Cited by
43 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献