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Oxidation‐reduction properties of thioredoxins and thioredoxin‐regulated enzymes
Author(s) -
Knaff David B.
Publication year - 2000
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.2000.1100304.x
Subject(s) - ferredoxin , ferredoxin thioredoxin reductase , thioredoxin , chloroplast , biochemistry , enzyme , fructose 1,6 bisphosphatase , malate dehydrogenase , chemistry , thioredoxin reductase , redox , dehydrogenase , reductase , biology , inorganic chemistry , gene
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‐regulated enzymes fructose‐1,6‐bisphosphatase (FBPase), phosphoribulokinase and NADP‐malate dehydrogenase. The effects of pH on the midpoint potentials of these chloroplast proteins have been measured so that the effect of the light‐induced increase in chloroplast stromal pH on the redox properties of the proteins can be calculated. Spectroscopic measurements on FTR and on an N‐ethylmaleimide‐modified derivative of the enzyme have been used to elucidate the role of the [4Fe‐4S] cluster of FTR during the reduction of the enzyme's active‐site disulfide by ferredoxin.