Journal
NANO LETTERS
Volume 9, Issue 9, Pages 3290-3295Publisher
AMER CHEMICAL SOC
DOI: 10.1021/nl9015705
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Funding
- European Union
- Deutsche Forschungsgerneinschaft
- Nanosystems Initiative Munich
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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 k(B)T. 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.
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