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Rik Chakraborty

Publications and source records attributed to Rik Chakraborty.

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Catalytic Crosstalk: Cooperative Enzyme Dynamics in Artificial Crowded Environments

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.

cond-mat.soft

Propagation of Enzyme-driven Active Fluctuations in Crowded Milieu

We investigated the energy transfer from active enzymes to their surroundings in crowded environments by measuring the diffusion of passive microscopic tracers in active solutions of ficoll and glycerol. Despite observing lower rates of substrate turnover and relatively smaller enhancement of passive tracer diffusion in artificial crowded media compared to those in aqueous solutions, we found a significantly higher relative diffusion enhancement in crowded environments in the presence of enzymatic activity. Our experimental observations, coupled with supporting analytical estimations, underscored the critical role of the intervening media in facilitating mechanical energy distribution around active enzymes.

cond-mat.soft