AI 中文总结
研究人工拥挤环境中过氧化氢酶和脲酶的催化串扰，通过实验发现二者共定位时相互增强催化活性和动态行为，建模提出模拟框架捕捉协同作用，揭示酶间合作可抵消拥挤有害影响维持酶效率。
AI 中文摘要
在细胞环境中，酶在密集拥挤条件下运作，常因限制底物扩散和关键构象动力学而阻碍催化效率。虽有报道称拥挤常导致酶催化活性受抑制，但细胞生物化学的持续效率暗示了这些分子间潜在的协同机制。在此，我们通过实验证明了过氧化氢酶和脲酶在人工拥挤环境中的催化串扰。结果显示，当在致密介质中共定位时，这些酶相互增强彼此的催化活性和动态行为。这种协同相互作用导致反应速率和迁移率净增加，表明酶组装体中出现了多体效应。将酶建模为二聚体活性粒子，我们提出了一个最小模拟框架，定性地捕捉到了观察到的协同作用。我们的发现表明，酶间合作可抵消拥挤的有害影响，为复杂生物环境中酶效率如何维持提供了见解。
英文摘要
In cellular environments, enzymes operate under densely crowded conditions that often hinder catalytic efficiency by limiting substrate diffusion and essential conformational dynamics. While reports suggest that crowding can often lead to inhibition of enzyme's catalytic activity, persistent efficiency of cellular biochemistry hints at underlying cooperative mechanisms among these molecules. Here, we experimentally demonstrate catalytic crosstalk between two enzymes - catalase and urease - in artificially crowded environments. Our results reveal that when co-localized in dense media, these enzymes mutually enhance each other's catalytic activity and dynamic behavior. This cooperative interaction leads to a net increase in reaction rates and mobility, suggesting an emergent many-body effect in enzyme assemblies. Modeling enzymes as dimeric active particles, we propose a minimal simulation framework that qualitatively captures the observed synergy. Our findings show that inter-enzyme cooperation can counteract the detrimental effects of crowding, offering insights into how enzymatic efficiency is sustained in complex biological milieu.
Comments6 pages, 5 figures
