Probing the chemistry of thioredoxin catalysis with force

Arun P. Wiita, Raul Perez-Jimenez, Kirstin A. Walther, Frauke Gräter, B. J. Berne, Arne Holmgren, Jose M. Sanchez-Ruiz and Julio M. Fernandez ()
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Arun P. Wiita: Department of Biological Sciences,
Raul Perez-Jimenez: Department of Biological Sciences,
Kirstin A. Walther: Department of Biological Sciences,
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,

Nature, 2007, vol. 450, issue 7166, 124-127

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.

Date: 2007
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DOI: 10.1038/nature06231

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