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Science 28 January 2000:
Vol. 287. no. 5453, pp. 655 - 658
DOI: 10.1126/science.287.5453.655
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Reports
Redox Signaling in Chloroplasts: Cleavage of Disulfides by an Iron-Sulfur Cluster
Shaodong Dai,
1*
Cristina Schwendtmayer,
2
Peter Schürmann,
2
S. Ramaswamy,
1
Hans Eklund
1
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.
1 Department of Molecular Biology, Swedish
University of Agricultural Sciences, Box 590, Biomedical Center, S-751
24 Uppsala, Sweden.
2 Laboratoire de Biochimie
Végétale, Université de Neuchâtel, CH-2007
Neuchâtel, Switzerland.
*
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}xray.bmc.uu.se
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