Manipulating single enzymes by an external harmonic force

Michael A. Lomholt*, Michael Urbakh, Ralf Metzler, Joseph Klafter

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


We study a Michaelis-Menten reaction for a single two-state enzyme molecule, whose transition rates between the two conformations are modulated by an harmonically oscillating external force. In particular, we obtain a range of optimal driving frequencies for changing the conformation of the enzyme, thereby controlling the enzymatic activity (i.e., product formation). This analysis demonstrates that it is, in principle, possible to obtain information about particular rates within the kinetic scheme.

Original languageEnglish
Article number168302
JournalPhysical Review Letters
Issue number16
StatePublished - 19 Apr 2007


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