期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 144, 期 11, 页码 4839-4844出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.1c12328
关键词
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资金
- National Science Foundation [CHE-1554717]
- National Institute of General Medical Sciences of the National Institutes of Health [DP2GM132681]
- Beckman Young Investigator Program
- Packard Fellowships for Science and Engineering
- Heising-Simons Faculty Fellows award
Recent studies have sparked debate over whether catalytic reactions enhance the diffusion coefficients of enzymes. Through high statistical analysis, it has been found that catalytic reactions do not affect the diffusion properties of hydrogenase, urease, aldolase, and alkaline phosphatase.
Recent studies have sparked debate over whethercatalytic reactions enhance the diffusion coefficientsDof enzymes.Through high statistics of the transient (600 mu s) displacements ofunhindered single molecules freely diffusing in common buffers, wehere quantifyDfor four enzymes under catalytic turnovers. Wethus formulate how similar to +/- 1% precisions may be achieved forD, andshow no changes in diffusivity for catalase, urease, aldolase, andalkaline phosphatase under the application of wide concentrationranges of substrates. Our single-molecule approach thus overcomespotential limitations and artifacts underscored by recent studies toshow no enhanced diffusion in enzymatic reactions
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