Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 96:1207-1213 (1991)
© 1991 American Society of Plant Biologists

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Metabolism and Enzymology

Ferredoxin and Ferredoxin-NADP Reductase from Photosynthetic and Nonphotosynthetic Tissues of Tomato 1

Laura S. Green2, Boihon C. Yee, Bob B. Buchanan, Kaeko Kamide, Yukika Sanada and Keishiro Wada

Department of Plant Biology, University of California, Berkeley, California 94720, Department of Biology, Faculty of Science, Kanazawa University, Marunouchi, Kanazawa 920 Japan

Ferredoxin and ferredoxin-NADP+ oxidoreductase (FNR) were purified from leaves, roots, and red and green pericarp of tomato (Lycopersicon esculentum, cv VFNT and cv Momotaro). Four different ferredoxins were identified on the basis of N-terminal amino acid sequence and charge. Ferredoxins I and II were the most prevalent forms in leaves and green pericarp, and ferredoxin III was the most prevalent in roots. Red pericarp of the VFNT cv yielded variable amounts of ferredoxins II and III plus a unique form, ferredoxin IV. Red pericarp of the Momotaro cv contained ferredoxins I, II, and IV. This represents the first demonstration of ferredoxin in a chromoplast-containing tissue. There were no major differences among the tomato ferredoxins in absorption spectrum or cytochrome c reduction activity. Two forms of FNR were present in tomato as judged by anion exchange chromatography and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. FNR II had a lower apparent relative molecular weight, a slightly altered absorption spectrum, and a lower specific activity for cytochrome c reduction than FNR I. FNR II could be a partially degraded form of FNR I. The FNRs from the different tissues of tomato plants all showed diaphorase activity, with FNR II being more active than FNR I. The presence of ferredoxin and FNR in heterotrophic tissues of tomato is consistent with the existence of a nonphotosynthetic ferredoxin/FNR redox pathway to support the function of ferredoxin-dependent enzymes.


2 Present address: CSIRO, Division of Plant Industry, GPO Box 1600, Canberra, Australian Capital Territory 2601 Australia.

1 This study was supported by grants from the National Science Foundation to L.S.G. (Postdoctoral Fellowship in Plant Biology) and to B.B.B. (DCB 8815980), and by a grant from the Japanese Ministry of Education, Science and Culture to K. W.




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