Structure and function of ferredoxin-NADP+-oxidoreductase

1 September 1988

journal article
review article
Published by Springer Nature in Photosynthesis Research

Vol. 17 (3) , 217-229
https://doi.org/10.1007/bf00035449

Abstract

The redox-enzyme ferredoxin-NADP-oxidoreductase has been shown to be activated by light and inactivated in the dark. This review will summarize recent data concerning the biochemical characterization of the enzyme compared to its in-vivo activation. Further-more the mechanism of this activation process is discussed as a conformational change caused by the light-driven proton gradient.

Keywords

This publication has 55 references indexed in Scilit:

The interaction of ferredoxin-linked sulfite reductase with ferredoxin
FEBS Letters, 1987
Chemical cross‐linking of ferredoxin to spinach thylakoids
FEBS Letters, 1987
Trimeric structure and other properties of the chloroplast reductase binding protein
FEBS Letters, 1985
Two sites of interaction of ferredoxin with thylakoids
FEBS Letters, 1985
Ferredoxin-sulfite reductase and ferredoxin-nitrite reductase activities in leaves of Pisum sativum: Changes during ontogeny and in vitro regulation by sulfide
Physiologia Plantarum, 1985
Association of ferredoxin‐NADP⁺ oxidoreductase with the chloroplast cytochrome b‐f complex
FEBS Letters, 1984
Interaction of ferredoxin-NADP+ oxidoreductase with triazine dyes a rapid purification method by affinity chromatography
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
On the conformation of reconstituted ferredoxin:NADP+ oxidoreductase in the thylakoid membrane. Studies via triplet lifetime and rotational diffusion with eosin isothiocyanate as label
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1982
Conformational changes of the isolated ferredoxin‐NADP‐oxidoreductase upon nucleotide binding as revealed by the triplet lifetime of bound eosin‐SCN
FEBS Letters, 1981
Role of Light in the Regulation of Chloroplast Enzymes
Annual Review of Plant Physiology, 1980