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Purification and characterization of a ferredoxin-NADP super(+) oxidoreductase-like enzyme from radish root tissues

An enzyme able to reduce cytochrome c via ferredoxin in the presence of NADPH, was isolated, purified from radish (Raphanus sativus var acanthiformis cultivar miyashige ) roots and characterized. The results suggest that the enzyme is similar to ferredoxin-NADP super(+) oxidoreductase from chloropla...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1990-01, Vol.93 (3), p.896-901
Main Authors: Morigasaki, S, Takata, K, Suzuki, T, Wada, K
Format: Article
Language:English
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Summary:An enzyme able to reduce cytochrome c via ferredoxin in the presence of NADPH, was isolated, purified from radish (Raphanus sativus var acanthiformis cultivar miyashige ) roots and characterized. The results suggest that the enzyme is similar to ferredoxin-NADP super(+) oxidoreductase from chloroplasts and cyanobacteria and is the key enzyme catalyzing the electron transport between NADPH, generated by the pentose phosphate pathway, and ferredoxin in plastids of plant heterotrophic tissues.
ISSN:0032-0889