Journal of the American Chemical Society · 2013 · 328 citations · 33 references
Life SciencesBiochemistryBiophysicsEnzyme MechanismEnzymologyNanobiotechnologyCatalytic MechanismsEnzyme BiophysicsEnzyme CatalysisEnzyme FunctionEnzyme-substrate RecognitionMolecular MachinesCatalase FunctionConcentration Gradient Driven TransportEnzyme Catalytic MechanismEnzyme MechanicsEnzyme Reaction MechanismsGlucose OxidaseHydrogen Peroxide GenerationSpatial Organization Of Enzymes
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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