Enzyme molecules as nanomotors

Samudra Sengupta, Krishna K. Dey, Hari S. Muddana, Tristan Tabouillot, Michael E. Ibele, Peter J. Butler, Ayusman Sen

Research output: Contribution to journalArticle

150 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1406-1414
Number of pages9
JournalJournal of the American Chemical Society
Issue number4
StatePublished - Jan 30 2013

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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    Sengupta, S., Dey, K. K., Muddana, H. S., Tabouillot, T., Ibele, M. E., Butler, P. J., & Sen, A. (2013). Enzyme molecules as nanomotors. Journal of the American Chemical Society, 135(4), 1406-1414. https://doi.org/10.1021/ja3091615