Structure and function of ferredoxin-NADP+-oxidoreductase |
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Authors: | Roland Pschorn Wolfgang Rühle Aloysius Wild |
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Institution: | (1) Institut für Allgemeine Botanik der Johannes Gutenberg-Universität, Saarstr. 21, D-6500 Mainz, Federal Republic of Germany |
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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.Abbreviations cyt
cytochrome
- fd
ferredoxin
- FNR1
large form of ferredoxin-NADP-oxidoreductase
- FNRox
oxidized FNR
- FNRred
reduced FNR
- FNRs
small form of FNR
- FNRsq
FNR-semiquinone |
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Keywords: | ferredoxin FNR activation mechanism proton gradient conformational change |
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