Oxidation-Reduction Properties of Chloroplast Thioredoxins, Ferredoxin:Thioredoxin Reductase, and Thioredoxin f-Regulated Enzymes

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 thioredoxi...

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Bibliographic Details
Published in:Biochemistry (Easton) 1999-04, Vol.38 (16), p.5200-5205
Main Authors: Hirasawa, Masakazu, Schürmann, Peter, Jacquot, Jean-Pierre, Manieri, Wanda, Jacquot, Pierre, Keryer, Eliane, Hartman, Fred C, Knaff, David B
Format: Article
Language:English
Subjects:
Animals
Chlamydomonas reinhardtii
Chlamydomonas reinhardtii - metabolism
Chloroplast Thioredoxins
Chloroplasts - enzymology
Chloroplasts - metabolism
Enzyme Activation - drug effects
Ferredoxin-thioredoxin reductase
Freshwater
Fructose-Bisphosphatase - metabolism
Hydrogen-Ion Concentration
Iron-Sulfur Proteins
Oxidation-Reduction
Oxidoreductases - metabolism
Pisum sativum - enzymology
Pisum sativum - metabolism
Plant Proteins - metabolism
Plant Proteins - physiology
Spinacia oleracea - enzymology
Spinacia oleracea - metabolism
thioredoxin
Thioredoxins - pharmacology
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Summary: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 (E m) values at pH 7.0 of −290 mV for both spinach and pea thioredoxin f, −300 mV for both C. reinhardtii and spinach thioredoxin m, −320 mV for spinach FTR, −290 mV for spinach PRK, −315 mV for pea FBPase, and −330 mV for spinach FBPase were obtained. With the exception of spinach FBPase, titrations showed a single two-electron component at all pH values tested. Spinach FBPase exhibited a more complicated behavior, with a single two-electron component being observed at pH values ≥ 7.0, but with two components being present at pH values
ISSN:0006-2960
1520-4995
DOI:10.1021/bi982783v