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Probing the chemistry of thioredoxin catalysis with force

Author

Listed:
  • Arun P. Wiita

    (Department of Biological Sciences,
    Graduate Program in Neurobiology and Behavior,)

  • Raul Perez-Jimenez

    (Department of Biological Sciences,)

  • Kirstin A. Walther

    (Department of Biological Sciences,
    Department of Physics,)

  • Frauke Gräter

    (Columbia University, New York, New York 10027, USA)

  • B. J. Berne

    (Columbia University, New York, New York 10027, USA)

  • Arne Holmgren

    (Medical Nobel Institute for Biochemistry, Karolinska Institutet, SE-171 77, Stockholm, Sweden)

  • Jose M. Sanchez-Ruiz

    (Facultad de Ciencias, Universidad de Granada, 18071, Granada, Spain)

  • Julio M. Fernandez

    (Department of Biological Sciences,)

Abstract

Thioredoxins catalyze disulphide bond reduction in all living organisms. Single-molecule force-clamp spectroscopy has revealed that there are two alternative forms of the catalytic reaction: the first requires a reorientation of the disulphide bond in the substrate and the second involves an elongation of the disulphide bond in the substrate.

Suggested Citation

  • Arun P. Wiita & Raul Perez-Jimenez & Kirstin A. Walther & Frauke Gräter & B. J. Berne & Arne Holmgren & Jose M. Sanchez-Ruiz & Julio M. Fernandez, 2007. "Probing the chemistry of thioredoxin catalysis with force," Nature, Nature, vol. 450(7166), pages 124-127, November.
    • Handle: RePEc:nat:nature:v:450:y:2007:i:7166:d:10.1038_nature06231
    DOI: 10.1038/nature06231
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