Redox Signaling in Chloroplasts: Cleavage of Disulfides by an Iron-Sulfur Cluster

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Science  28 Jan 2000:
Vol. 287, Issue 5453, pp. 655-658
DOI: 10.1126/science.287.5453.655

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Light generates reducing equivalents in chloroplasts that are used not only for carbon reduction, but also for the regulation of the activity of chloroplast enzymes by reduction of regulatory disulfides via the ferredoxin:thioredoxin reductase (FTR) system. FTR, the key electron/thiol transducer enzyme in this pathway, is unique in that it can reduce disulfides by an iron-sulfur cluster, a property that is explained by the tight contact of its active-site disulfide and the iron-sulfur center. The thin, flat FTR molecule makes the two-electron reduction possible by forming on one side a mixed disulfide with thioredoxin and by providing on the opposite side access to ferredoxin for delivering electrons.

  • * Present address: Department of Biological Sciences, 1392 Lilly Hall of Life Sciences, Purdue University, West Lafayette, IN 47907, USA.

  • Present address: Department of Biochemistry, University of Iowa, 51 Newton Road, Iowa City, IA 52242–1109, USA.

  • To whom correspondence should be addressed. E-mail: hasse{at}

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