Novel forms of ferredoxin and ferredoxin-NADP reductase from spinach roots.
Ferredoxin and the enzyme catalyzing its reduction by NADPH, ferredoxin-NADP reductase (ferredoxin-NADP+ oxidoreductase or FNR), were found to be present in roots of spinach (Spinacia oleracea). Localization experiments with endosperm of germinating castor beans (Ricinus communis), a classical nonphotosynthetic tissue for cell fractionation studies, confirmed that ferredoxin and FNR are localized in the plastid fraction. Both proteins were purified from spinach roots and found to resemble their leaf counterparts in activity, spectral properties, and complex formation, but to differ in amino acid composition and amino terminal sequence. The results indicate that the primary structures of the FNR and ferredoxin of spinach roots differ from that of the corresponding leaf proteins. Together with earlier findings, the present results provide evidence that nonphotosynthetic plastids, including those of roots, are capable of reducing ferredoxin with heterotrophically generated NADPH.
Morigasaki
S
S
Department of Biology, Faculty of Science, Kanazawa University, Ishikawa, Japan.
Takata
K
K
Sanada
Y
Y
Wada
K
K
Yee
B C
BC
Shin
S
S
Buchanan
B B
BB
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005287:Ferredoxin-NADP Reductase / Q000302:isolation & purification* / Q000378:metabolism; D005288:Ferredoxins / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D013053:Spectrophotometry
D000596:Amino Acids; D005288:Ferredoxins; D005287:Ferredoxin-NADP Reductase