Light-driven enzyme catalysis: Ultrafast mechanisms and biochemical implications

He, YongLe, Barone, Marco, Meech, Stephen R., Lukacs, Andras and Tonge, Peter J. (2025) Light-driven enzyme catalysis: Ultrafast mechanisms and biochemical implications. Biochemistry, 64 (12). pp. 2491-2505. ISSN 0006-2960

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Abstract

Light-activated enzymes are an important class of biocatalysts in which light energy is directly converted into biochemical activity. In most cases the light absorbing group is the isoalloxazine ring of an embedded flavin cofactor and in general two types of mechanism are in operation depending on whether the excited chromophore directly participates in catalysis or where photoexcitation triggers conformational changes that modulate the activity of a downstream output partner. This review will summarize studies on DNA photolyase, fatty acid photodecarboxylase (FAP), the monooxygenase PqsL, and flavin-dependent ene-reductases, where flavin radicals generated by excitation are directly used in the reactions catalyzed by these enzymes, and the blue light using FAD (BLUF) and light oxygen voltage (LOV) domain photoreceptors where flavin excitation drives ultrafast structural changes that ultimately result in enzyme activation. Recent advances in methods such as time-resolved spectroscopy and structural imaging have enabled unprecedented insight into the ultrafast dynamics that underly the mechanism of light-activated enzymes, and here we highlight how understanding ultrafast protein dynamics not only provides valuable insights into natural phototransduction processes but also opens new avenues for enzyme engineering and consequent applications in fields such as optogenetics.

Item Type:	Article
Additional Information:	Funding information: This work was supported by grants to P.J.T. from the National Institutes of Health (GM149297) and the National Science Foundation (MCB-1817837) and to S.R.M. from the EPSRC (EP/N033647/1). A.L. acknowledges funding from the Hungarian National Research and Innovation Office (K-137557) and was supported by PTE ÁOK-KA-2021. Y.H. was supported by a National Institutes of Health Chemistry–Biology Interface Training Grant (T32GM092714) and M.B. was supported by an Abroad Fellowship (31189) from Associazione Italiana per la Ricerca sul Cancro (AIRC).
Uncontrolled Keywords:	biochemistry,1*,review ,/dk/atira/pure/subjectarea/asjc/1300/1303
Faculty \ School:	Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
UEA Research Groups:	Faculty of Science > Research Groups > Centre for Photonics and Quantum Science Faculty of Science > Research Groups > Chemistry of Light and Energy
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	09 Jul 2025 10:30
Last Modified:	15 Jul 2025 08:33
URI:	https://ueaeprints.uea.ac.uk/id/eprint/99871
DOI:	10.1021/acs.biochem.5c00039

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