Isolation and characterization of two ferredoxin-NADP+ reductases from Spirulina platensis.
Two ferredoxin-NADP+ reductases (FNRs I and II) [EC 1.6.7.1] were purified from a blue-green alga, Spirulina platensis, by (NH4)2SO4 fractionation, gel filtration on Sephadex G-100 and DEAE-Sephadex A-50 chromatography. FNRs I and II were both FAD-containing enzymes with molecular weights of 33,000, and could photochemically reduce NADP+ to the same extent in the presence of S. platensis ferredoxin, using FNR-depleted membrane fragments of S. platensis. They had similar physical and enzymatic properties, except for chemical properties such as the amino (N)-terminal sequences and the patterns of their peptide maps. The significance of the presence of two FNRs in S. platensis as as of the multiple forms found in other organisms is discussed.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000460:Chlorophyta / Q000201:enzymology*; D005287:Ferredoxin-NADP Reductase / Q000302:isolation & purification* / Q000378:metabolism; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000032:analysis
D000596:Amino Acids; D007527:Isoenzymes; D010446:Peptide Fragments; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases