Triggering enzymatic activity with force

Hermann Gumpp, Elias M. Puchner, Julia L. Zimmermann, Ulrich Gerland, Hermann E. Gaub, Kerstin Blank

Research output: Contribution to journalArticlepeer-review

52 Scopus citations


Integrating single molecule force spectroscopy with fluorescence-based techniques allows the manipulation of an enzyme with a periodic stretching and relaxation protocol while simultaneously monitoring its catalytic activity. After releasing the stretching force we observe a higher probability for enzymatic activity at a time of 1. 7 s. A detailed theoretical analysis reveals that the relaxation from the force-induced enzyme conformation to the observed active conformation follows a cascade reaction with several steps and a free energy difference of at least 8 kBT. Our study clearly points out the direct influence of force on enzymatic activity and opens up a new way to study and manipulate (bio)catalytic reactions at the single molecule level.

Original languageEnglish (US)
Pages (from-to)3290-3295
Number of pages6
JournalNano letters
Issue number9
StatePublished - Sep 9 2009


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