无阻单分子的位移统计显示酶反应中没有增强的扩散。
Displacement Statistics of Unhindered Single Molecules Show no Enhanced Diffusion in Enzymatic Reactions.
机构信息
Department of Chemistry, University of California, Berkeley, California 94720, United States.
Chan Zuckerberg Biohub, San Francisco, California 94158, United States.
出版信息
J Am Chem Soc. 2022 Mar 23;144(11):4839-4844. doi: 10.1021/jacs.1c12328. Epub 2022 Mar 8.
Abstract
Recent studies have sparked debate over whether catalytic reactions enhance the diffusion coefficients of enzymes. Through high statistics of the transient (600 μs) displacements of unhindered single molecules freely diffusing in common buffers, we here quantify for four enzymes under catalytic turnovers. We thus formulate how ∼ ±1% precisions may be achieved for , and show no changes in diffusivity for catalase, urease, aldolase, and alkaline phosphatase under the application of wide concentration ranges of substrates. Our single-molecule approach thus overcomes potential limitations and artifacts underscored by recent studies to show no enhanced diffusion in enzymatic reactions.
摘要
最近的研究引发了关于催化反应是否能提高酶的扩散系数的争论。通过对在常见缓冲液中自由扩散的无阻碍单分子的瞬态（600μs）位移进行高统计，我们在这里量化了四种酶在催化循环下的扩散系数。因此，我们制定了如何实现 ±1%精度的方案，并表明在广泛的底物浓度范围内，过氧化氢酶、脲酶、醛缩酶和碱性磷酸酶的扩散率没有变化。因此，我们的单分子方法克服了最近研究中强调的潜在限制和人为因素，表明酶反应中没有增强扩散。
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