Antigenic similarities between ferredoxin-dependent nitrite reductase and glutamate synthase fromChlamydomonas reinhardtii |
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| Institution: | 1. Departamento de Bioquímica Vegetal y Biología Molecular, Facultad de Química, Seville Spain;2. Biochemistry Department, Rothamsted Experimental Station, AFRC Institute for Arable Crops Research, Harpenden U.K.;1. Key Laboratory of Algal Biology of the Chinese Academy of Sciences, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China;2. University of Chinese Academy of Sciences, Beijing 100049, China;3. Egerton University, Department of Environmental Science, Egerton 536-20115, Kenya;1. Shaanxi Key Laboratory of Environmental Engineering, Key Laboratory of Northwest Water Resource, Environment and Ecology, MOE, Xi’an University of Architecture and Technology, Xi’an 710055, China;2. School of Municipal and Environmental Engineering, Xi’an University of Architecture and Technology, Xi’an 710055, China;1. Faculdade de Ciências Médicas de Minas Gerais, Alameda Ezequiel Dias 275, Belo Horizonte, MG, Brazil;2. Instituto Medico Legal, Rua Nícias Continentino, 1291, Belo Horizonte, MG, Brazil |
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| Abstract: | Polyclonal antisera were prepared against ferredoxin-nitrite reductase (EC 1.7.7.1) and ferredoxin-glutamate synthase (glutamate synthase (ferredoxin); EC 1.4.7.1) from the green algaChlamydomonas reinhardtii. The anti-glutamate synthase antibodies recognized both glutamate synthase and nitrite reductase, but inhibited only the ferredoxin-linked activity of the latter enzyme and not the activity dependent on methyl viologen. Analogously, the anti-nitrite reductase antibodies recognized glutamate synthase and nitrite reductase but the first enzyme was only poorly inhibited. Free ferredoxin protected the nitrite reductase against its inactivation by anti-glutamate synthase antibodies. These results indicate that the ferredoxin-dependent glutamate synthase and nitrite reductase from this alga share common antigenic determinants, and that these are located at the ferrodoxin-binding domains. |
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