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Structural snapshots along the reaction pathway of ferredoxin–thioredoxin reductase

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  • 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
    Present addresses: Department of Chemistry, University of Oslo, PB 1033, Blindern, 0315 Oslo, Norway (R.F.); Fondation pour Recherches Médicales, CH-1211 Genève, Switzerland (D.A.G.); Biochemisches Institut, Universität Zürich, CH-8057 Zürich, Switzerland (F.B.); College of Pharmacy, Medical Center, University of Cincinnati, Cincinnati, Ohio 45267-0004, USA (W.M.).)

  • Dominique A. Glauser

    (Université de Neuchâtel, Laboratoire de Biologie Moléculaire et Cellulaire, Rue Emile Argand 11, CH-2009 Neuchâtel, Switzerland
    Present addresses: Department of Chemistry, University of Oslo, PB 1033, Blindern, 0315 Oslo, Norway (R.F.); Fondation pour Recherches Médicales, CH-1211 Genève, Switzerland (D.A.G.); Biochemisches Institut, Universität Zürich, CH-8057 Zürich, Switzerland (F.B.); College of Pharmacy, Medical Center, University of Cincinnati, Cincinnati, Ohio 45267-0004, USA (W.M.).)

  • Florence Bourquin

    (Université de Neuchâtel, Laboratoire de Biologie Moléculaire et Cellulaire, Rue Emile Argand 11, CH-2009 Neuchâtel, Switzerland
    Present addresses: Department of Chemistry, University of Oslo, PB 1033, Blindern, 0315 Oslo, Norway (R.F.); Fondation pour Recherches Médicales, CH-1211 Genève, Switzerland (D.A.G.); Biochemisches Institut, Universität Zürich, CH-8057 Zürich, Switzerland (F.B.); College of Pharmacy, Medical Center, University of Cincinnati, Cincinnati, Ohio 45267-0004, USA (W.M.).)

  • Wanda Manieri

    (Université de Neuchâtel, Laboratoire de Biologie Moléculaire et Cellulaire, Rue Emile Argand 11, CH-2009 Neuchâtel, Switzerland
    Present addresses: Department of Chemistry, University of Oslo, PB 1033, Blindern, 0315 Oslo, Norway (R.F.); Fondation pour Recherches Médicales, CH-1211 Genève, Switzerland (D.A.G.); Biochemisches Institut, Universität Zürich, CH-8057 Zürich, Switzerland (F.B.); College of Pharmacy, Medical Center, University of Cincinnati, Cincinnati, Ohio 45267-0004, USA (W.M.).)

  • 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)

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.

Suggested Citation

  • Shaodong Dai & Rosmarie Friemann & Dominique A. Glauser & Florence Bourquin & Wanda Manieri & Peter Schürmann & Hans Eklund, 2007. "Structural snapshots along the reaction pathway of ferredoxin–thioredoxin reductase," Nature, Nature, vol. 448(7149), pages 92-96, July.
    • Handle: RePEc:nat:nature:v:448:y:2007:i:7149:d:10.1038_nature05937
    DOI: 10.1038/nature05937
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    Cited by:

    1. Yu Zheng & Katsuyuki Sakai & Kohei Watanabe & Hiroshi Takagi & Yumi Sato-Shiozaki & Yuko Misumi & Yohei Miyanoiri & Genji Kurisu & Toshihiko Nogawa & Ryo Takita & Shunji Takahashi, 2024. "Iron-sulphur protein catalysed [4+2] cycloadditions in natural product biosynthesis," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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