Fullerene-Based Mimics of Biocatalysts Show Remarkable Activity and Modularity.

Date

2021-09-29

Author

Gülseren, Gülcihan
Saylam, Aytül
Marıon, Antoıne
Özçubukçu, Salih

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The design of catalysts with greater control over catalytic activity and stability is a major challenge with substantial impact on fundamental chemistry and industrial applications. Due to their unparalleled diversity, selectivity, and efficiency, enzymes are promising models for next-generation catalysts, and considerable efforts have been devoted to incorporating the principles of their mechanisms of action into artificial systems. We report a heretofore undocumented catalyst design that introduces fullerenes to the field of biocatalysis, which we refer to as fullerene nanocatalysts, and that emulates enzymatic active sites through multifunctional self-assembled nanostructures. As a proof-of-concept, we mimicked the reactivity of hydrolases using fullerene nanocatalysts functionalized with the basic components of the parent enzyme with remarkable activity. Owing to the versatile amino acid-based functionalization repertoire of fullerene nanocatalysts, these next-generation carbon/biomolecule hybrids have potential to mimic the activity of other families of enzymes and, therefore, offer new perspectives for the design of biocompatible, high-efficiency artificial nanocatalysts.

Subject Keywords

fullerene, fullerenol, biocatalysis, enzyme mimic, amino acids, molecular dynamics, QM/MM

URI

https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85116027300&origin=inward
https://hdl.handle.net/11511/93435

Journal

ACS applied materials & interfaces

DOI

https://doi.org/10.1021/acsami.1c11516

Collections

Department of Chemistry, Article

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Citation Formats

G. Gülseren, A. Saylam, A. Marıon, and S. Özçubukçu, “Fullerene-Based Mimics of Biocatalysts Show Remarkable Activity and Modularity.,” ACS applied materials & interfaces, vol. 13, no. 38, pp. 45854–45863, 2021, Accessed: 00, 2021. [Online]. Available: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85116027300&origin=inward.