0000000000082695

AUTHOR

Roland Pschorn

showing 2 related works from this author

The Influence of the Proton Gradient on the Activation of Ferredoxin-NADP+-oxidoreductase by Light

1988

Ferredoxin-NADP+-oxidoreductase (FNR, EC 1.18.1.2) has been shown to be activated by light within a few seconds during dark-light transitions and inactivated in the dark. In previous papers this could be pointed out by the correlation of cytochrome f induction kinetics to the rate of NADP-photoreduction and the variable fluorescence. The present study deals with the role of the proton gradient during the activation process. The transition from an inactive to an active form is followed continuously in an in situ system. The steady-state rate of NADP-photoreduction is affected only by ionophores which inhibit a formation of the proton gradient, but not by inhibitors of the electric field. It …

ChemistryBiophysicsLight activationElectrochemical gradientElectron transport chainGeneral Biochemistry Genetics and Molecular BiologyFerredoxin:NADP+ oxidoreductaseZeitschrift für Naturforschung C
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Structure and function of ferredoxin-NADP+-oxidoreductase

1987

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.

chemistry.chemical_classificationConformational changeChemistryCell BiologyPlant ScienceGeneral MedicineBiochemistryLight effectFerredoxin:NADP+ oxidoreductaseStructure and functionEnzymeBiochemistrysense organsElectrochemical gradientFerredoxin—NADP(+) reductaseFerredoxinPhotosynthesis Research
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