title: Enhanced diffusion, chemotaxis, and pumping by active enzymes: progress toward an organizing principle of molecular machines.
abstract: Active enzymes diffuse more rapidly than inactive enzymes. This phenomenon may be due to catalysis-driven conformational changes that result in "swimming" through the aqueous solution. Recent additional work has demonstrated that active enzymes can undergo chemotaxis toward regions of high substrate concentration, whereas inactive enzymes do not, and, further, that active enzymes immobilized at surfaces can directionally pump liquids. In this Perspective, I will discuss these phenomena in light of Purcell's work on directed motion at low Reynold's number and in the context of microscopic reversibility. The conclusions suggest that a deep understanding of catalytically driven enhanced diffusion of enzymes and related phenomena can lead toward a general organizing principle for the design, characterization, and operation of molecular machines.
authors.affiliation: Department of Physics, The University of Maine , 5709 Bennett Hall, Orono, Maine 04469-5709, United States.
authors.forename: R Dean
authors.initials: RD
authors.lastname: Astumian
mesh_terms: D002633:Chemotaxis; D004798:Enzymes / Q000302:isolation & purification*; D046210:Microfluidic Analytical Techniques
chemical_list: D004798:Enzymes