4.8 Article

Enzyme Molecules as Nanomotors

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 135, Issue 4, Pages 1406-1414

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ja3091615

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Funding

  1. Penn State MRSEC under NSF [DMR-0820404]

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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.

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