Enzyme–metal nanobiohybrids: coordination-controlled nanostructure formation and emerging catalytic function

Enzyme–metal nanoparticle hybrids (nanobiohybrids) have emerged as a versatile class of bioinspired materials that integrate the molecular recognition and catalytic selectivity of enzymes with the physicochemical and catalytic properties of metal nanostructures. These systems enable the in situ generation and organization of metal nanoparticles within or around protein scaffolds under mild conditions, with their composition, size, morphology, and spatial distribution influenced by factors such as enzyme identity, metal precursor, metal-to-protein ratio, and synthesis conditions. In this review, we examine the main strategies used to construct enzyme–metal nanobiohybrids, ranging from enzyme-guided nanoparticle formation to single-enzyme confinement and surface-immobilized architectures. We discuss how protein–metal interactions contribute to the organization and stabilization of the inorganic phase and summarize current insights into the coordination, reduction, nucleation, and growth processes involved in nanoparticle formation. Particular attention is given to how the resulting hybrid architectures influence catalytic activity, selectivity, stability, and substrate accessibility. We further review recent advances in the application of nanobiohybrids as multifunctional catalysts for fine and pharmaceutical chemistry, including selective transformations and cascade reactions, as well as their emerging applications in environmental remediation and the control of biological contaminants. Overall, enzyme–metal nanobiohybrids provide a promising platform for integrating biological recognition with inorganic catalytic functionality, while offering opportunities for the rational design of advanced materials for sustainable catalysis and related applications.