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

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.

Original languageEnglish (US)
Pages (from-to)1406-1414
Number of pages9
JournalJournal of the American Chemical Society
Volume135
Issue number4
DOIs
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