PubMed · 7579659
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1995. Protein engineering.. https://doi.org/10.1016/0958-1669(95)80079-4
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Photobiocatalysis integrates enzymatic catalysis with photochemistry, enabling challenging radical transformations with high selectivity under mild conditions. Early developments in this field were largely driven by the discovery that enzyme-bound cofactors can form photoactive charge-transfer complexes with substrates, thereby initiating radical chemistry upon light irradiation. Recent advances, however, have substantially expanded the mechanistic landscape of photobiocatalysis through diverse mechanisms. This review summarizes major developments in photobiocatalysis reported since 2024. Rather than cataloging individual reactions, we focus on the fundamental mechanisms of radical generation and interception within enzyme active sites, and discuss how these mechanistic principles guide the discovery, engineering, and design of enzymes for new-to-nature photobiocatalysis.
Proteins are capable of fulfilling two important features of any likely system of bioelectronics: the ability to recognise other molecules with exquisite specificity, and the ability to self-assemble, in vivo and in vitro, to generate an astonishing variety of three-dimensional structures. Much current work is aimed at the redesign of existing proteins, either as an end in itself or as a means of developing the knowledge-base necessary for the ab initio design of novel proteins. This type of study has been greatly facilitated by the discovery of the modular or domain structure of many proteins, leading to concepts of protein manipulation as a kind of molecular Lego.
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