Designing and Engineering Enzymes for New-to-Nature Photobiocatalysis.

Jie Feng, Chang-Liang Zhu, Mao-Lin Li

Abstract readReview

In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Jie FengState Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Frontiers Science Center for New Organic Matter, Nankai University, Tianjin, China.

Chang-Liang ZhuState Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Frontiers Science Center for New Organic Matter, Nankai University, Tianjin, China.

Mao-Lin LiState Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Frontiers Science Center for New Organic Matter, Nankai University, Tianjin, China. maolin@nankai.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photobiocatalysis, an interdisciplinary frontier integrating chemistry, biology, and catalysis, drives enzymatic catalysis from natural reactions to new-to-nature transformations via protein engineering and photochemistry. This review centers on enzyme classes, covering nine key families: fatty acid photodecarboxylases (FAPs), nicotinamide-dependent reductases, flavin-dependent "ene"-reductases (EREDs), and others like artificial photoenzymes. We detail photoenzymatic development, mechanisms, and protein engineering for reactivity expansion. Despite enzymes' superior stereocontrol, their reaction scope is narrower than small-molecule catalysts. Future exploration of universal activation mechanisms and AI-assisted engineering will expand photobiocatalysis' potential for sustainable chiral synthesis and green chemistry.

Indexed as

BiocatalysisEnzymesProtein EngineeringCarboxy-LyasesCatalysisPhotochemical ProcessesCarboxy-LyasesEnzymesArtificial photoenzymesMetalloenzymaticNature cofactor-dependent enzymesNew-to-naturePhotobiocatalysis

Identifiers

PMID42681175

DOI10.1021/jacs.4c03087

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.