Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz

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Gewählte Publikation:

Edman, L; Foldes-Papp, Z; Wennmalm, S; Rigler, R.
The fluctuating enzyme: a single molecule approach
CHEM PHYS. 1999; 247(1): 11-22. Doi: 10.1016/S0301-0104(99)00098-1
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Co-Autor*innen der Med Uni Graz
Földes-Papp Zeno
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Abstract:
The excess of structural degrees of freedom in a protein enzyme opens questions about the conformational homogeneity. We studied single horseradish peroxidase enzyme turnovers by fluorescence spectroscopy. Application of a two-state dynamic model to the measured data shows exponential product dissociation kinetics, but a large distribution of rates for the enzyme to form the enzyme-product complex. The experiments show that in addition to the peroxidative cycle thermodynamic fluctuation phenomena on a wide range of time scales affect enzyme activity. (C) 1999 Elsevier Science B.V. All rights reserved.

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