ArticleACS catalysis2020
Photochemical Mechanism of Light-Driven Fatty Acid Photodecarboxylase.
Article in ACS catalysis, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 122 citations in OpenAlex.
- Light as a master switch: a critical review of photonanozymes from design to applications.Advanced biotechnology · 2026Review
- Flavin Catalysts in Organic Synthesis.Angewandte Chemie (International ed. in English) · 2026Review
- Molecular Mechanism of the Catalytic Radical Termination in Fatty Acid Photodecarboxylase.Journal of the American Chemical Society · 2026Article
- Structural Principles of Covalent Flavin Modification in Oxidoreductases.Biochemistry · 2026Review
- Establishing the Fatty Acid PhotodecarboxylaseACS catalysis · 2026Article
- On the Origin of the Red-Shifted Flavin Absorption Spectra in Fatty Acid Photodecarboxylase.The journal of physical chemistry. B · 2026Article
- Designing and Engineering Enzymes for New-to-Nature Photobiocatalysis.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Photoenzymatic Decarboxylation to Produce Hydrocarbon Fuels: A Critical Review.Molecular biotechnology · 2025Review
- Efficient and selective energy transfer photoenzymes powered by visible light.Nature chemistry · 2025Article
- Light-Driven Enzyme Catalysis: Ultrafast Mechanisms and Biochemical Implications.Biochemistry · 2025Review
- Transitioning enzyme catalysis towards photocatalysis.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025Review
- A Foundational Shift in Models for Enzyme Function.Journal of the American Chemical Society · 2025Review
- Exploring the Increased Activity of the Blue Light-Dependent Photoenzyme Fatty Acid Photodecarboxylase under Violet Light.ACS catalysis · 2025Article
- Article
- Azobenzene-Based Photoswitchable Substrates for Advanced Mechanistic Studies of Model Haloalkane Dehalogenase Enzyme Family.ACS catalysis · 2024Article
- Stereodivergent photobiocatalytic radical cyclization through the repurposing and directed evolution of fatty acid photodecarboxylases.Nature chemistry · 2024Article
- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
- Photobiocatalytic Strategies for Organic Synthesis.Chemical reviews · 2023Review
- Temporal and spatial resolution of distal protein motions that activate hydrogen tunneling in soybean lipoxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Co-production of biofuel, bioplastics and biochemicals during extended fermentation of Halomonas bluephagenesis.Microbial biotechnology · 2023Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fatty acid photodecarboxylase (FAP) is a promising target for the production of biofuels and fine chemicals. It contains a flavin adenine dinucleotide cofactor and catalyzes the blue-light-dependent decarboxylation of fatty acids to generate the corresponding alkane. However, little is known about the catalytic mechanism of FAP, or how light is used to drive enzymatic decarboxylation. Here, we have used a combination of time-resolved and cryogenic trapping UV-visible absorption spectroscopy to characterize a red-shifted flavin intermediate observed in the catalytic cycle of FAP. We show that this intermediate can form below the "glass transition" temperature of proteins, whereas the subsequent decay of the species proceeds only at higher temperatures, implying a role for protein motions in the decay of the intermediate. Solvent isotope effect measurements, combined with analyses of selected site-directed variants of FAP, suggest that the formation of the red-shifted flavin species is directly coupled with hydrogen atom transfer from a nearby active site cysteine residue, yielding the final alkane product. Our study suggests that this cysteine residue forms a thiolate-flavin charge-transfer species, which is assigned as the red-shifted flavin intermediate. Taken together, our data provide insights into light-dependent decarboxylase mechanisms catalyzed by FAP and highlight important considerations in the (re)design of flavin-based photoenzymes.
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Registered trials
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.