Enzyme molecules as nanomotors

J Am Chem Soc. 2013 Jan 30;135(4):1406-14. doi: 10.1021/ja3091615. Epub 2013 Jan 22.

Abstract

Using fluorescence correlation spectroscopy, we show that the diffusive movements of catalase enzyme molecules increase in the presence of the substrate, hydrogen peroxide, in a concentration-dependent manner. Employing a microfluidic device to generate a substrate concentration gradient, we show that both catalase and urease enzyme molecules spread toward areas of higher substrate concentration, a form of chemotaxis at the molecular scale. Using glucose oxidase and glucose to generate a hydrogen peroxide gradient, we induce the migration of catalase toward glucose oxidase, thereby showing that chemically interconnected enzymes can be drawn together.

Publication types

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

MeSH terms

  • Catalase / chemistry*
  • Catalase / metabolism
  • Glucose / chemistry*
  • Glucose / metabolism
  • Glucose Oxidase / chemistry*
  • Glucose Oxidase / metabolism
  • Hydrogen Peroxide / chemistry*
  • Hydrogen Peroxide / metabolism
  • Nanostructures / chemistry*
  • Urease / chemistry*
  • Urease / metabolism

Substances

  • Hydrogen Peroxide
  • Glucose Oxidase
  • Catalase
  • Urease
  • Glucose