Redox Control of Glutathione and Thioredoxin Reductases

  • Juan López-Barea
  • Jose Antonio Bárcena
Part of the NATO ASI Series book series (NSSA, volume 7)


Redox interconversion was discovered in the seventies, when activation of several photosynthetic enzymes by reduced thioredoxin (1), and redox control of NO 3 -, NO 2 -, and NADP+-reductases were first described (2). Regulation of many enzymes by -SH/-SS- exchange has been recently reported, either by direct reaction with low Mw thiols or disulfides, or in a process catalyzed by thiol-transferases (3). Glutathione and thioredoxin reductases are two FAD-containing NADP+-disulfide oxidoreductases, using NADPH to reduce the -SS- groups of glutathione and thioredoxin (1, 4, 5). Both enzymes and their reduced products connect the NADP+/NADPH couple with the pools of low and high Mw thiols and disulfides; then, a general regulatory mechanism could be envisaged if the activities of such enzymes were redox controlled.


Glutathione Reductase Mixed Disulfide Yeast Enzyme Full Reactivation Diaphorase Activity 


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Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Juan López-Barea
    • 1
  • Jose Antonio Bárcena
    • 1
  1. 1.Depto. de Bioquímica y Biología Molecular (F. Veterinaria)Universidad de CórdobaCórdobaEspaña

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