Lookup NU author(s): Dorota Kostrz,
Professor Christopher Dennison
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Single-molecule measurements are a valuable tool for revealing details of enzyme mechanisms by enabling observation of unsynchronized behavior. However, this approach often requires immobilizing the enzyme on a substrate, a process which may alter enzyme behavior. We apply a microfluidic trapping device to allow, for the first time, prolonged solution-phase measurement of single enzymes in solution. Individual redox events are observed for single molecules of a blue nitrite reductase and are used to extract the microscopic kinetic parameters of the proposed catalytic cycle. Changes in parameters as a function of substrate concentration are consistent with a random sequential substrate binding mechanism.
Author(s): Goldsmith RH, Tabares LC, Kostrz D, Dennison C, Aartsma TJ, Canters GW, Moerner WE
Publication type: Article
Publication status: Published
Journal: Proceedings of the National Academy of Sciences
Print publication date: 18/10/2011
ISSN (print): 0027-8424
ISSN (electronic): 1091-6490
Publisher: National Academy of Sciences
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