F0628
Ferredoxin-NADP+ Reductase from Spinacia oleracea (spinach)
lyophilized powder, ≥15 units/mg solid, secondary activity: ≥10 units/mg solid NADPH diaphorase
Synonym(s):
Ferridoxin-NADP+ oxidoreductase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Product Name
Ferredoxin-NADP+ Reductase from Spinacia oleracea (spinach), lyophilized powder, ≥15 units/mg solid, secondary activity: ≥10 units/mg solid NADPH diaphorase
form
lyophilized powder
specific activity
≥15 units/mg solid
foreign activity
NADH diaphorase activity ≤10 units/mg solid
storage temp.
−20°C
Quality Level
Biochem/physiol Actions
Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP(H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria.
Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP(H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria.
General description
Ferredoxin-NADP+ Reductase is a ferredoxin-soluble partner with a molar ratio to PSI of 0.9 and 3.
Other Notes
One unit will reduce 1.0 millimole of cytochrome C per min at pH 7.5 at 25 °C in the presence of spinach ferredoxin and NADP.
Application
Ferredoxin-NADP+ Reductase from Spinacia oleracea (spinach) has been used to test the effect of potential protein partners on the activity of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)−CP12 preparation. It has also been used in standard assay conditions for phycocyanobilin:ferredoxin oxidoreductase (PcyA) enzyme assay.
Ferredoxin-NADP+ Reductase was used in in vitro ferredoxin-dependent desaturation of fatty acids in cyanobacterial thylakoid membranes. It was also used to regulate glyceraldehyde-3-phosphate dehydrogenase.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Manuel Twachtmann et al.
The Plant cell, 24(7), 2979-2991 (2012-07-19)
To adapt to different light intensities, photosynthetic organisms manipulate the flow of electrons through several alternative pathways at the thylakoid membrane. The enzyme ferredoxin:NADP(+) reductase (FNR) has the potential to regulate this electron partitioning because it is integral to most
[Laparocentesis in clinical traumatology].
V V Kuz'menko et al.
Khirurgiia, (6)(6), 50-54 (1986-06-01)
CRYSTALLIZATION OF FERREDOXIN-TPN REDUCTASE AND ITS ROLE IN THE PHOTOSYNTHETIC APPARATUS OF CHLOROPLASTS.
M SHIN et al.
Biochemische Zeitschrift, 338, 84-96 (1963-01-01)
Shin, M.
Methods in Enzymology, 23, 441-441 (1971)
Sara Baroni et al.
Biochemistry, 51(18), 3819-3826 (2012-04-24)
Plasmodium falciparum ferredoxin-NADP(+) reductase (FNR) is a FAD-containing enzyme that, in addition to be a promising target of novel antimalarial drugs, represents an excellent model of plant-type FNRs. The cofactor specificity of FNRs depends on differences in both k(cat) and
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