Letter abstract
Nature Materials 1, 173 - 177 (2002)
Published online: 27 October 2002 | doi:10.1038/nmat761
Subject Categories: Biological materials | Molecular electronics | Sensors and biosensors | Nanoscale materials
Control of a biomolecular motor-powered nanodevice with an engineered chemical switch
Haiqing Liu1, Jacob J. Schmidt1, George D. Bachand2, Shahir S. Rizk3, Loren L. Looger3, Homme W. Hellinga3 & Carlo D. Montemagno1
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 systems1, 2, 3, 4. The cytoplasmic F1 fragment of the adenosine triphosphate synthase (F1-ATPase) can function as an ATP-fuelled rotary motor4, 5, 6, 7 and has been integrated into self-assembled nanomechanical systems as a mechanical actuator4, 8. 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.
- Department of Bioengineering, University of California, Los Angeles, California 90095, USA
- Present address: Biomolecular Materials and Interfaces, Sandia National Laboratories, PO Box 5800, MS 1413, Albuquerque, New Mexico 87185-1413, USA
- Department of Biochemistry, Box 3711, Duke University Medical Center, Durham, North Carolina 27710, USA
Correspondence to: Carlo D. Montemagno1 e-mail: cdm@seas.ucla.edu
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