Ferredoxin-thioredoxin reductase: a catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation
Abstract
The mechanism by which the ferredoxin-thioredoxin system activates the target enzyme, NADP-malate dehydrogenase, was investigated by analyzing the sulfhydryl status of individual protein components with (/sup 14/C)iodoacetate and monobromobimane. The data indicate that ferredoxin-thioredoxin reductase (FTR)--an iron-sulfur enzyme present in oxygenic photosynthetic organisms--is the first member of a thiol chain that links light to enzyme regulation. FTR possesses a catalytically active dithiol group localized on the 13 kDa (similar) subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin m. The reduced thioredoxin m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive (S-S) to an active (SH) form. The means by which FTR is able to combine electrons (from photoreduced ferredoxin) with protons (from the medium) to reduce its active disulfide group remains to be determined.
- Authors:
- Publication Date:
- Research Org.:
- Universite de Paris-Sud, Orsay, France
- OSTI Identifier:
- 6075597
- Resource Type:
- Journal Article
- Journal Name:
- Arch. Biochem. Biophys.; (United States)
- Additional Journal Information:
- Journal Volume: 256:1
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; FERREDOXIN; BIOLOGICAL FUNCTIONS; OXIDOREDUCTASES; REDOX REACTIONS; CARBON 14 COMPOUNDS; CATALYSIS; ELECTRONS; PHOTOSYNTHESIS; PLANTS; PROTONS; STOICHIOMETRY; TOLUENE; TRACER TECHNIQUES; ALKYLATED AROMATICS; AROMATICS; BARYONS; CHEMICAL REACTIONS; ELEMENTARY PARTICLES; ENZYMES; FERMIONS; FUNCTIONS; HADRONS; HYDROCARBONS; ISOTOPE APPLICATIONS; LABELLED COMPOUNDS; LEPTONS; METALLOPROTEINS; NUCLEONS; ORGANIC COMPOUNDS; PHOTOCHEMICAL REACTIONS; PROTEINS; SYNTHESIS; 550201* - Biochemistry- Tracer Techniques
Citation Formats
Droux, M, Miginiac-Maslow, M, Jacquot, J P, Gadal, P, Crawford, N A, Kosower, N S, and Buchanan, B B. Ferredoxin-thioredoxin reductase: a catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation. United States: N. p., 1987.
Web. doi:10.1016/0003-9861(87)90458-9.
Droux, M, Miginiac-Maslow, M, Jacquot, J P, Gadal, P, Crawford, N A, Kosower, N S, & Buchanan, B B. Ferredoxin-thioredoxin reductase: a catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation. United States. https://doi.org/10.1016/0003-9861(87)90458-9
Droux, M, Miginiac-Maslow, M, Jacquot, J P, Gadal, P, Crawford, N A, Kosower, N S, and Buchanan, B B. 1987.
"Ferredoxin-thioredoxin reductase: a catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation". United States. https://doi.org/10.1016/0003-9861(87)90458-9.
@article{osti_6075597,
title = {Ferredoxin-thioredoxin reductase: a catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation},
author = {Droux, M and Miginiac-Maslow, M and Jacquot, J P and Gadal, P and Crawford, N A and Kosower, N S and Buchanan, B B},
abstractNote = {The mechanism by which the ferredoxin-thioredoxin system activates the target enzyme, NADP-malate dehydrogenase, was investigated by analyzing the sulfhydryl status of individual protein components with (/sup 14/C)iodoacetate and monobromobimane. The data indicate that ferredoxin-thioredoxin reductase (FTR)--an iron-sulfur enzyme present in oxygenic photosynthetic organisms--is the first member of a thiol chain that links light to enzyme regulation. FTR possesses a catalytically active dithiol group localized on the 13 kDa (similar) subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin m. The reduced thioredoxin m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive (S-S) to an active (SH) form. The means by which FTR is able to combine electrons (from photoreduced ferredoxin) with protons (from the medium) to reduce its active disulfide group remains to be determined.},
doi = {10.1016/0003-9861(87)90458-9},
url = {https://www.osti.gov/biblio/6075597},
journal = {Arch. Biochem. Biophys.; (United States)},
number = ,
volume = 256:1,
place = {United States},
year = {Wed Jul 01 00:00:00 EDT 1987},
month = {Wed Jul 01 00:00:00 EDT 1987}
}