The ferredoxin-NADP+ oxidoreductase-binding protein is not the 17-kDa component of the cytochrome b/f complex.
The complex between ferredoxin-NADP+ oxidoreductase and its proposed membrane-binding protein (Vallejos, R. H., Ceccarelli, E., and Chan, R. (1984) J. Biol. Chem. 259, 8048-8051) was isolated from spinach thylakoids and compared with isolated cytochrome b/f complex containing associated ferredoxin NADP+ oxidoreductase (Clark, R. D., and Hind, G. (1983) J. Biol. Chem. 258, 10348-10354). There was no immunological cross-reactivity between the 17.5-kDa binding protein and an antiserum raised against the 17-kDa polypeptide of the cytochrome complex. Association of ferredoxin-NADP+ oxidoreductase with the binding protein or with the thylakoid membrane gave an allotopic shift in the pH profile of diaphorase activity, as compared to the free enzyme. This effect was not seen in enzyme associated with the cytochrome b/f complex. Identification of the 17.5-kDa binding protein as the 17-kDa component of the cytochrome b/f complex is ruled out by these results.
D001665:Binding Sites; D002793:Cholic Acids; D002846:Chromatography, Affinity; D003429:Cross Reactions; D003580:Cytochromes / Q000032:analysis*; D045348:Cytochromes f; D005287:Ferredoxin-NADP Reductase / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D007163:Immunosorbent Techniques; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis*; D010944:Plants / Q000201:enzymology
D002793:Cholic Acids; D003580:Cytochromes; D045348:Cytochromes f; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate