Evidence map›Paper›PMID 36260429›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Ultrafast Dynamics and Catalytic Mechanism of Fatty Acid Photodecarboxylase.

Ruiqi Wu, Xiankun Li, Lijuan Wang, Dongping Zhong

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

Who cites it

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Transitioning enzyme catalysis towards photocatalysis.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Ultrafast Dynamics and Catalytic Mechanism of Fatty Acid Photodecarboxylase.Angewandte Chemie (International ed. in English) · 2022
    Article
  10. Article
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

4 authors.

Ruiqi WuDepartment of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Xiankun LiDepartment of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Lijuan WangDepartment of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Dongping ZhongDepartment of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.ORCID 0000-0001-9381-8992

Funding

Biological dynamics for protein properties and functionsR35GM144047 · NIGMS · OHIO STATE UNIVERSITY · PI ZHONG, DONGPING · 2022 to 2023
$934k
NIGMS NIH HHS R35 GM144047
6 · The paper itself

Abstract

Fatty acid photodecarboxylase is a newly discovered flavin photoenzyme that converts a carboxylic acid into a hydrocarbon and a carbon dioxide molecule through decarboxylation. The enzymatic reactions are poorly understood. In this study, we carefully characterized its dynamic evolution with femtosecond spectroscopy. We observed initial electron transfer from the substrate to the flavin cofactor in 347 ps with a stretched dynamic behavior and subsequently captured the critical carbonyloxy radical. The dominant process following this step was decarboxylation in 5.8 ns to form an alkyl radical and a carbon dioxide molecule. We further identified the absorption bands of two carbonyloxy and alkyl radical intermediates. The overall enzymatic quantum efficiency determined by our obtained timescales is 0.81, consistent with the steady-state value. The results are essential to the elucidation of the enzyme mechanism and catalytic photocycle, providing a molecular basis for potential design of flavin-based artificial photoenzymes.

Indexed as

Deoxyribodipyrimidine Photo-LyaseCarbon DioxideCatalysisFatty AcidsFlavinsCarbon DioxideDeoxyribodipyrimidine Photo-LyaseFatty AcidsFlavinsCatalytic PhotocycleElectron TransferFlavin PhotoenzymesHydrocarbon FormationPhotodecarboxylation

Identifiers

PMID36260429
PMCPMC9729393

What OpenQuestion holds

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Registered trials

None linked

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.