Control of a biomolecular motor-powered nanodevice with an engineered chemical switch

Nat Mater. 2002 Nov;1(3):173-7. doi: 10.1038/nmat761.


The biophysical and biochemical properties of motor proteins have been well-studied, but these motors also show promise as mechanical components in hybrid nano-engineered systems. The cytoplasmic F(1) fragment of the adenosine triphosphate synthase (F1-ATPase) can function as an ATP-fuelled rotary motor and has been integrated into self-assembled nanomechanical systems as a mechanical actuator. Here we present the rational design, construction and analysis of a mutant F1-ATPase motor containing a metal-binding site that functions as a zinc-dependent, reversible on/off switch. Repeated cycles of zinc addition and removal by chelation result in inhibition and restoration, respectively, of both ATP hydrolysis and motor rotation of the mutant, but not of the wild-type F1 fragment. These results demonstrate the ability to engineer chemical regulation into a biomolecular motor and represent a critical step towards controlling integrated nanomechanical devices at the single-molecule level.

Publication types

  • Comparative Study
  • Evaluation Study
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Actins / physiology
  • Adenosine Triphosphatases / drug effects
  • Adenosine Triphosphatases / metabolism*
  • Bacillus / genetics
  • Bacillus / metabolism
  • Cloning, Molecular
  • Enzyme Inhibitors / metabolism
  • Equipment Design
  • Equipment Failure Analysis / methods
  • Feedback
  • Homeostasis / physiology
  • Materials Testing / methods
  • Models, Molecular
  • Molecular Motor Proteins / chemical synthesis*
  • Molecular Motor Proteins / genetics
  • Molecular Motor Proteins / physiology*
  • Motion
  • Movement / physiology*
  • Mutagenesis, Site-Directed
  • Nanotechnology / instrumentation
  • Nanotechnology / methods*
  • Sensitivity and Specificity
  • Zinc / metabolism*
  • Zinc / pharmacology


  • Actins
  • Enzyme Inhibitors
  • Molecular Motor Proteins
  • Adenosine Triphosphatases
  • Zinc