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Enzyme Molecules as Nanomotors
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.
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Cited by
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Merindol, R., & Walther, A. (2017) · Chemical Society Reviews · doi:10.1039/c6cs00738d · Cited by 533
Mimicking the Cell: Bio-Inspired Functions of Supramolecular Assemblies
Tu, Y., Peng, F., Adawy, A., Men, Y., Abdelmohsen, L. K. E. A., & Wilson, D. A. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00344 · Cited by 316
Sustained enzymatic activity and flow in crowded protein droplets
Testa, A., Dindo, M., Rebane, A. A., Nasouri, B., Style, R. W., Golestanian, R., Dufresne, E. R., & Laurino, P. (2021) · Nature Communications · doi:10.1038/s41467-021-26532-0 · Cited by 144
Metadata
- Authors
- Sengupta, S., Dey, K. K., Muddana, H. S., Tabouillot, T., Ibele, M. E., Butler, P. J., & Sen, A.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2013-01-22
- Volume
- 135
- Issue
- 4
- Pages
- 1406-1414
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2332621967
- Cited by
- 321
- References
- 0
- FWCI
- 15.60
- Type
- journal article
- Language
- en
- Open access
- closed
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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. https://doi.org/10.1021/ja3091615
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