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Photosystem I-independent oxygenic photosynthesis in cyanobacteria
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Immobilized Ferredoxin-NADP+ Reductase: Preparation and Properties
The Journal of Biochemistry, 1982Immobilized ferredoxin-NADP+ reductase (FNR) was prepared by coupling reaction of CNBr-Sepharose 4B with the spinach enzyme. The immobilized FNR was found to retain the activity of complex formation with ferredoxin as well as the enzymatic activities such as NADPH-diaphorase and NADPH-cytochrome c reductase activities.
M, Shin +4 more
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On the Enzymology of Ferredoxin-NADP Reductase
Biochemical and Biophysical Research Communications, 1972Properties and location of this Enzyme (EC 1.6.99.4 or/and 1.6.1.1) within the photosynthetic electron transport chain were described in detail (AVRON & JAGENDORF 1956, KEISTER et al 1960, 1962, SHIN & ARNON 1965, SHIN 1968, FORTI & ZANETTI 1967). The enzyme reduces NADP with ferredoxin as the electron donor (reductase activity).
N, Nelson, J, Neumann
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Resolution and reconstitution of spinach ferredoxin-NADP+ reductase
Biochemical and Biophysical Research Communications, 1978Abstract The apoprotein from spinach ferredoxin-NADP + reductase was prepared by treatment with 3 M calcium chloride. This procedure caused complete removal of the FAD prosthetic group together with considerable denaturation of the apoprotein. Thus, the recovery of total activity upon reconstitution with FAD was only 30%.
G, Bookjans, A, San Pietro, P, Böger
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Crystals of Anabaena PCC 7119 ferredoxin-NADP+ reductase
Journal of Molecular Biology, 1991Crystals of ferredoxin-NADP+ reductase (FNR) from the cyanobacterium Anabaena PCC 7119 are grown in the presence of polyethylene glycol 6000 and beta-octyl glucoside. They belong to the hexagonal system. The cell parameters are a = b = 87.8 A, c = 92.7 A, space group P6(1) or P6(5), and a Vm of 3.0 A3/dalton for one molecule of 36,000 daltons per ...
L, Serre +4 more
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Molecular heterogeneity of ferredoxin-NADP+ reductase from spinach leaves
Biochemical and Biophysical Research Communications, 1983Highly purified ferredoxin-NADP+ reductase from spinach leaves showed at least eight different protein bands in the electrofocused gel. All of them were catalytically active and were adsorbed on a ferredoxin-Sepharose 4B affinity column. The N-terminal amino acid sequence of the main component species was analyzed by the automatic Edman degradation ...
H, Hasumi, E, Nagata, S, Nakamura
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Molecular heterogeneity of ferredoxin-NADP+ reductase from spinach leaves
Biochimica et Biophysica Acta (BBA) - Enzymology, 1977Ferredoxin-NADP+ reductase (NADPH: ferredoxin oxidoreductase, EC 1.6.7.1) from spinach leaves has been purified according to a new procedure. The enzyme shows the presence of five molecular forms as identified by isoelectric focusing, namely a, b, c, d and e with pI values of 6.0, 5.5, 5.2, 5.0 and 4.8, respectively.
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Interaction of ferredoxin and ferredoxin-NADP reductase with thylakoids
Archives of Biochemistry and Biophysics, 1983Ferredoxin-NADP reductase accounts for about 50% of the NADPH diaphorase activity of spinach leaf homogenates. The enzyme is bound to thylakoid membranes, but can be slowly extracted by aqueous buffers. Ferredoxin-NADP reductase can be extracted from the membranes by a 1- to 2-min treatment with a low concentration of trypsin. This treatment completely
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