Origin of Metal Cluster Tuning Enzyme Activity at the Bio-Nano Interface.

Abstract

Detailed understanding of how the bio-nano interface orchestrates the function of both biological components and nanomaterials remains ambiguous. Here, through a combination of experiments and molecular dynamics simulations, we investigated how the interface between Candida Antarctic lipase B and palladium (Pd) nanoparticles (NPs) tunes the structure, dynamics, and catalysis of the enzyme. Our simulations show that the metal binding to protein is a shape matching behavior and there is a transition from saturated binding to unsaturated binding along with the increase in the size of metal NPs. When we engineered the interface with the polymer, not only did the critical size of saturated binding of metal NPs become larger, but also the disturbance of the metal NPs to the enzyme function was reduced. In addition, we found that an enzyme–metal interface engineered with the polymer can boost bio-metal cascade reactions via substrate channeling. Understanding and control of the bio-nano interface at the molecular level enable us to rationally design bio-nanocomposites with prospective properties.