title: Triggering enzymatic activity with force.
abstract: 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.
authors: Lehrstuhl für Angewandte Physik and Center for Nanoscience, Center for Integrated Protein Science Munich, LMU München, D-80799 München, Germany.
authors: Hermann
authors: H
authors: Gumpp
authors: Elias M
authors: EM
authors: Puchner
authors: Julia L
authors: JL
authors: Zimmermann
authors: Ulrich
authors: U
authors: Gerland
authors: Hermann E
authors: HE
authors: Gaub
authors: Kerstin
authors: K
authors: Blank
mesh_terms: D002384:Catalysis; D005452:Fluoresceins / Q000737:chemistry; D005453:Fluorescence; D005656:Fungal Proteins; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D036103:Nanotechnology
chemical_list: D005452:Fluoresceins; D005656:Fungal Proteins; C024098:6-carboxyfluorescein; C093616:6-carboxyfluorescein diacetate; C045132:4-carboxyfluorescein; C084577:5-carboxyfluorescein diacetate; D008049:Lipase; C431349:lipase B, Candida antarctica