Journal of the American Chemical Society 2013-01-30

Enzyme molecules as nanomotors.

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

Index: J. Am. Chem. Soc. 135(4) , 1406-14, (2013)

Full Text: HTML

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.


Related Compounds

Related Articles:

RESOLFT nanoscopy with photoswitchable organic fluorophores.

2015-01-01

[Sci. Rep. 5 , 17804, (2015)]

Compartmentalization of the chick cerebellar cortex based on the link between the striped expression pattern of aldolase C and the topographic olivocerebellar projection.

2015-09-01

[J. Comp. Neurol. 523 , 1886-912, (2015)]

Spatial Control of Epsin-induced Clathrin Assembly by Membrane Curvature.

2015-06-05

[J. Biol. Chem. 290 , 14267-76, (2015)]

TUT7 controls the fate of precursor microRNAs by using three different uridylation mechanisms.

2015-07-02

[EMBO J. 34(13) , 1801-15, (2015)]

Quantitative localization microscopy: effects of photophysics and labeling stoichiometry.

2015-01-01

[PLoS ONE 10 , e0127989, (2015)]

More Articles...