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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Liu, H; Schmidt, JJ; Bachand, GD; Rizk, SS; Looger, LL; Hellinga, HW; Montemagno, CD

Published Date

  • November 2002

Published In

Volume / Issue

  • 1 / 3

Start / End Page

  • 173 - 177

PubMed ID

  • 12618806

International Standard Serial Number (ISSN)

  • 1476-1122

Digital Object Identifier (DOI)

  • 10.1038/nmat761


  • eng

Conference Location

  • England