Characterization of a ferredoxin:NADP+ oxidoreductase from a nonphotosynthetic plant tissue.
A flavoprotein with properties similar to those of ferredoxin:NADP+ oxidoreductases found in the leaves of higher plants has been purified to apparent homogeneity from bean sprouts, a nonphotosynthetic plant tissue. The absorbance and circular dichroism spectra of the bean sprout protein are similar to those of spinach leaf ferredoxin:NADP+ oxidoreductase and an antibody raised against the spinach enzyme recognized the bean sprout enzyme. The bean sprout enzyme catalyzed ferredoxin-dependent electron transfer from NADPH to equine cytochrome c at a high rate but, unlike the spinach enzyme, exhibited little NADPH to 2,6-dichlorophenol indophenol diaphorase activity. The bean sprout enzyme forms a 1:1 electrostatically stabilized complex with ferredoxins isolated from either bean sprouts or spinach leaves.
Hirasawa
M
M
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock 79409-1061.
Chang
K T
KT
Knaff
D B
DB
D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D007887:Fabaceae / Q000201:enzymology; D005287:Ferredoxin-NADP Reductase / Q000302:isolation & purification / Q000378:metabolism*; D005779:Immunodiffusion; D007700:Kinetics; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010788:Photosynthesis; D010944:Plants / Q000201:enzymology*; D010946:Plants, Medicinal; D013045:Species Specificity; D013053:Spectrophotometry
D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases