作者: Eric Gaymard , Laurence Franchini , Wanda Manieri , Erhard Stutz , Peter Schürmann
DOI: 10.1016/S0168-9452(00)00310-1
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摘要: Abstract Ferredoxin:thioredoxin reductase (FTR) is a heterodimeric FeS containing disulfide involved in the light-dependent activation of photosynthetic enzymes. We have designed dicistronic construct for heterologous expression this nucleus encoded chloroplast protein Escherichia coli . The coding sequences two mature subunits been inserted tandem into vector pET-3d. This correctly translated yielding soluble, perfectly functional FTR. recombinant enzyme composed both subunits, contains cluster as evidenced by its spectral properties and indistinguishable from isolated leaves capacity to activate fructose-1,6-bisphosphatase, one well known light activated enzymes Calvin cycle.