Structural snapshots along the reaction pathway of ferredoxin–thioredoxin reductase

Shaodong Dai (), Rosmarie Friemann, Dominique A. Glauser, Florence Bourquin, Wanda Manieri, Peter Schürmann and Hans Eklund
Additional contact information
Shaodong Dai: Howard Hughes Medical Institute, National Jewish Medical and Research Center & University of Colorado Health Sciences Center, 1400 Jackson Street, Denver, Colorado 80206, USA
Rosmarie Friemann: Swedish University of Agricultural Sciences, Biomedical Centre, Box 590, S-75124 Uppsala, Sweden
Dominique A. Glauser: Université de Neuchâtel, Laboratoire de Biologie Moléculaire et Cellulaire, Rue Emile Argand 11, CH-2009 Neuchâtel, Switzerland
Florence Bourquin: Université de Neuchâtel, Laboratoire de Biologie Moléculaire et Cellulaire, Rue Emile Argand 11, CH-2009 Neuchâtel, Switzerland
Wanda Manieri: Université de Neuchâtel, Laboratoire de Biologie Moléculaire et Cellulaire, Rue Emile Argand 11, CH-2009 Neuchâtel, Switzerland
Peter Schürmann: Université de Neuchâtel, Laboratoire de Biologie Moléculaire et Cellulaire, Rue Emile Argand 11, CH-2009 Neuchâtel, Switzerland
Hans Eklund: Swedish University of Agricultural Sciences, Biomedical Centre, Box 590, S-75124 Uppsala, Sweden

Nature, 2007, vol. 448, issue 7149, 92-96

Abstract: The X-ray structures of ferredoxin–thioredoxin reductase (FDR) in its one- and two-electron-reduced intermediate states and four complexes in the pathway are solved, including the ternary ferredoxin–FTR–thioredoxin complex. These results provide a structural framework for understanding the mechanism of disulphide reduction by an iron-sulphur enzyme.

Date: 2007
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DOI: 10.1038/nature05937

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