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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Published inJournal of the American Chemical Society Vol. 135; no. 4; pp. 1406 - 1414
Main Authors Sengupta, Samudra, Dey, Krishna K, Muddana, Hari S, Tabouillot, Tristan, Ibele, Michael E, Butler, Peter J, Sen, Ayusman
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 30.01.2013
Subjects
Catalase - chemistry
Catalase - metabolism
Glucose - chemistry
Glucose - metabolism
Glucose Oxidase - chemistry
Glucose Oxidase - metabolism
Hydrogen Peroxide - chemistry
Hydrogen Peroxide - metabolism
Nanostructures - chemistry
Urease - chemistry
Urease - metabolism
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0002-7863
1520-5126
DOI:10.1021/ja3091615