Enzyme Molecules as Nanomotors.

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 th...

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Detalles Bibliográficos
Publicado en:Journal of the American Chemical Society Vol. 135; no. 4; pp. 1406 - 1415
Autores principales: Sengupta, Samudra, Dey, Krishna K., Muddana, Hari S., Tabouillot, Tristan, Ibele, Michael E., Butler, Peter J., Sen, Ayusman
Formato: Artículo
Publicado: American Chemical Society 1/30/2013
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Acceso en línea:Ver este registro en EBSCOhost
Descripción
Sumario: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.