Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f-regulated enzymes.

  title={Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f-regulated enzymes.},
  author={Masakazu Hirasawa and Peter Schürmann and Jean-Pierre Jacquot and Wanda Manieri and Pierre Jacquot and Eliane K{\'e}ryer and Fred C. Hartman and David B. Knaff},
  volume={38 16},
Oxidation-reduction midpoint potentials were determined, as a function of pH, for the disulfide/dithiol couples of spinach and pea thioredoxins f, for spinach and Chlamydomonas reinhardtii thioredoxins m, for spinach ferredoxin:thioredoxin reductase (FTR), and for two enzymes regulated by thioredoxin f, spinach phosphoribulokinase (PRK) and the fructose-1,6-bisphosphatases (FBPase) from pea and spinach. Midpoint oxidation-reduction potential (Em) values at pH 7.0 of -290 mV for both spinach and… Expand
Distinct electron transfer from ferredoxin-thioredoxin reductase to multiple thioredoxin isoforms in chloroplasts.
It is shown that FTR prepared here was enzymatically active and suitable for uncovering biochemical features of chloroplast redox regulation, and a series of redox state determinations indicated that allchloroplast Trx isoforms are commonly reduced by FTR; however, significantly different efficiencies were evident. Expand
Oxidation-reduction properties of thioredoxins and thioredoxin-regulated enzymes.
Oxidation-reduction midpoint potentials have been measured for the two chloroplast thioredoxins, thioredoxin f and m, for ferredoxin:thioredoxin reductase (FTR) and for the thioredoxin-regulatedExpand
The Structure and Function of the Ferredoxin/Thioredoxin System in Photosynthesis
The demonstration that thioredoxin could function in regulation grew out of CO2 assimilation experiments initiated more than thirty years ago with isolated chloroplasts. This work ultimately led toExpand
The chloroplast 2-cysteine peroxiredoxin functions as thioredoxin oxidase in redox regulation of chloroplast metabolism
The results show that the 2-CysPrx serves as electron sink in the thiol network important to oxidize reductively activated proteins and represents the missing link in the reversal of thioredoxin-dependent regulation. Expand
Thioredoxin-dependent Redox Regulation of Chloroplastic Phosphoglycerate Kinase from Chlamydomonas reinhardtii*
It is concluded that CrPGK1 might constitute an additional light-modulated Calvin-Benson cycle enzyme with a low activity in the dark and a TRX-dependent activation in the light, and the formation of the disulfide is proposed to impose structural constraints in the C-terminal domain of the enzyme that may lower its catalytic efficiency. Expand
Characterization of Ferredoxin:Thioredoxin Reductase Modified by Site-directed Mutagenesis*
Heteroduplexes form non-covalent complexes with ferredoxin demonstrating the ability of FTR to simultaneously dock thioredoxin and ferredoxins, which is in accord with the proposed reaction mechanism and the structural analyses. Expand
Biochemical Characterization of Glutaredoxins from Chlamydomonas reinhardtii Reveals the Unique Properties of a Chloroplastic CGFS-type Glutaredoxin*
Both GRXs proved to be very efficient catalysts of A4-glyceraldehyde-3-phosphate dehydrogenase deglutathionylation, whereas cytosolic and chloroplastic thioredoxins were inefficient. Expand
Thioredoxin-dependent Redox Regulation of Chloroplastic
The redox features of the Calvin-Benson enzyme phosphoglycerate kinase (PGK1) from the eukaryotic green alga Chlamydomonas reinhardtii are characterized, and it is concluded that CrPGK 1 might constitute an additional light-modulated Calvin- Benson cycle enzyme with a low activity in the dark and a TRX-dependent activation in the light. Expand
The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux
  • J. König, M. Baier, +4 authors K. Dietz
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2002
The function of the 2-Cys Prx is therefore not confined to its role in the water–water cycle pathway for energy dissipation in photosynthesis but also mediates peroxide detoxification in the plastids during the dark phase. Expand
Ferredoxin:thioredoxin Reductase: Disulfide Reduction Catalyzed via Novel Site-specific [4Fe–4S] Cluster Chemistry
Structural and spectroscopic studies of ferredoxin and a chemically modified form, termed NEM–FTR, are summarized, which provide the basis for a novel mechanism for disulfide cleavage in two one-electron steps involving site-specific [4Fe–4S] cluster chemistry. Expand


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XI International Photosynthesis Congress Abstracts
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