Structure and Function of Ferredoxin-NADP Reductase Complex
In 1963, Shin et al. (1) first isolated ferredoxin-NADP reductase (FNR, EC. 220.127.116.11) in crystalline form from spinach and demonstrated that the crystallized enzyme reduced NADP when it was added back together with ferredoxin to illuminated chloroplasts from which “built-in” FNR had been removed. In this experiment, however, a very large excess of crystallized FNR was required to restore the original activity. This requirement of excess FNR indicates that membrane-bound FNR is more functional in the NADP photoreduction than the FNR added in a soluble state. So our recent interest has been focused on the structure and function of membrane-bound FNR. We have found that two molecules of a small form of FNR, FNR-S, was connected with a new thylakoid protein, connectein, to form a large form of FNR, FNR-L. The FNR-L was anchored on the surface of thylakoids via a base protein to constitute a ferredoxin-NADP reductase complex.
KeywordsBase Protein Spinach Chloroplast Thylakoid Protein Diaphorase Activity Japan Scientific Society
Unable to display preview. Download preview PDF.
- 1.Shin, M., Tagawa, K. and Arnon, D. I. (1963) Biochem, Z. 338, 84–96Google Scholar
- 3.Shin, M. and Oshino, R. (1980) in Flavins and Flavoproteins (Yagi, K. and Yamano, T., eds.), pp.537–541, Japan Scientific Societies Press, Tokyo and University Park Press, Baltimore.Google Scholar
- 4.Shin, M., Ishida, H. and Nozaki, Y. (1985) Plant Cell Physiol. 26, 559–663Google Scholar
- 6.Nozaki, Y. and Shin, M. (1985) Physiol. Veg. 23, 627–633Google Scholar