Laboratory of Biochemistry and Molecular Biology

Redox Regulation of Enzymes in Chloroplasts


 

Our group worked on the ferredoxin/thioredoxin system, a light-dependent redox system regulating the activitiy of key enzymes in chloroplasts. We have purified, cloned and overexpressed the proteins involved in the regulatory cascade, i.e. ferredoxin:thioredoxin reductase (FTR), a novel Fe-S protein, the thioredoxins f and m and one of the target enzymes, the fructose 1,6-bisphosphatase. These proteins are used to study their structure and the mechanism of redox regulation.

The three-dimensional structures of FTR and the two chloroplast thioredoxins have been solved in collaboration with Shaodong Dai in Uppsala (http://alpha2.bmc.uu.se/~dai/) and Guido Capitani (now at the University of Zürich, Biochemisches Institut, capitani@biocfebs.unizh.ch) at the Biozentrum in Basel, respectively. The FTR structure was published in Science in January 2000.

We have also made significant progress in the understanding of the reaction mechanism of the FTR which is studied in collaboration with Michael K. Johnson (http://www.uga.edu/cms/FacMKJ.html) at the Center for Metalloenzyme Studies, University of Georgia in Athens, USA.
 

The group was headed by Peter Schürmann (peter.schurmann@unine.ch), who is now retired but still actively finishing up his research.

Recent publications on the subject:

The local collaborators are indicated in bold

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Last modifications : 22nd February 2005

(editor: Jean-Marc Neuhaus)