Ferredoxin:NADP oxidoreductase of Cyanophora paradoxa: purification, partial characterization, and N-terminal amino acid sequence.
The ferredoxin:NADP+ oxidoreductase of the protist Cyanophora paradoxa, as a descendant of a former symbiotic consortium, an important model organism in view of the Endosymbiosis Theory, is the first enzyme purified from a formerly original endocytobiont (cyanelle) that is found to be encoded in the nucleus of the host. This cyanoplast enzyme was isolated by FPLC (19% yield) and characterized with respect to the uv-vis spectrum, pH optimum (pH 9), molecular mass of 34 kDa, and an N-terminal amino acid sequence (24 residues). The enzyme shows, as known from other organisms, molecular heterogeneity. The N-terminus of a further ferredoxin:NADP+ oxidoreductase polypeptide represents a shorter sequence missing the first four amino acids of the mature enzyme.
Gebhart
U B
UB
Botanical Institute, University of Tübingen, Germany.
Maier
T L
TL
Stevanović
S
S
Bayer
M G
MG
Schenk
H E
HE
D000595:Amino Acid Sequence; D005075:Biological Evolution; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D003956:Dialysis; D056890:Eukaryota / Q000235:genetics* / Q000378:metabolism; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry / Q000302:isolation & purification*; D005420:Flavoproteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D015388:Organelles / Q000201:enzymology; D013559:Symbiosis
D005420:Flavoproteins; D005287:Ferredoxin-NADP Reductase