Early View e202301424
Review

Photocatalytic Structures for Protein Modifications

Dr. Zhengyi Liu

Dr. Zhengyi Liu

Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, Sendai, 980- 8578 Japan

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Ass. Prof. Yasunori Okamoto

Ass. Prof. Yasunori Okamoto

Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, Sendai, 980- 8578 Japan

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Ass. Prof. Shinichi Sato

Corresponding Author

Ass. Prof. Shinichi Sato

Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, Sendai, 980- 8578 Japan

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First published: 12 January 2024

Graphical Abstract

This review delves into photochemical strategies, which have gained attention for their biocompatibility and precision. It explores various catalysts, including photoredox catalysts, energy transfer catalysts, and genetically encoded photocatalysts, shedding light on their unique attributes, mechanisms, applications, and future potential. This comprehensive analysis illuminates the exciting developments in protein chemical modifications.

Abstract

The chemical modification of proteins serves as a fundamental tool for understanding biological processes and enables the design of biofunctional materials. Among the available methodologies, photochemical strategies have garnered significant attention because of their remarkable biocompatibility and precise spatiotemporal reaction control. Developing novel reactions tailored to specific applications necessitates a comprehensive understanding of photoreactive properties, including catalyst structures, appropriate modifiers, and reaction conditions. This review discusses chemical modifications of proteins using an array of catalysts, including photoredox catalysts for single-electron transfer (SET), catalysts for energy transfer, long-wavelength excitable photocatalysts, genetically encoded photocatalysts, and artificial metalloenzymes. The discussion covers the unique attributes, mechanisms, practical applications, and future prospects of each catalyst-driven reaction, shedding light on the evolving landscape of protein chemical modifications.

Conflict of interest

The authors declare no conflict of interest.