ArticleNature communications2017
Capturing an initial intermediate during the P450nor enzymatic reaction using time-resolved XFEL crystallography and caged-substrate.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
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- A simple and practical approach for protein serial crystallography using grease matrix and large-area support film.Journal of synchrotron radiation · 2026Article
- Precisely Timed On-Demand Droplet Ejection and Collision in Free Space for Controlled Reaction Initiation.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Structure-guided identification of denitrification inhibitors to mitigate agricultural NNature communications · 2026Article
- Radiation-induced peroxide rupture and its temperature-dependent repair probed by homogeneous X-ray irradiation.Acta crystallographica. Section D, Structural biology · 2026Article
- Sensitive detection of structural dynamics using a statistical framework for comparative crystallography.Science advances · 2025Article
- Tracking Protein Motions using Serial Femtosecond Crystallography with X-Ray Free-Electron Laser.Current protocols · 2025Article
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- Photocontrolled Release of Urea Enables the Detection of Urea-Urease Intermediates by Cryo-FTIR.Angewandte Chemie (International ed. in English) · 2025Article
- Macromolecular crystallography and biology at the Linac Coherent Light Source.Journal of synchrotron radiation · 2025Article
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- Damage before destruction? X-ray-induced changes in single-pulse serial femtosecond crystallography.IUCrJ · 2025Article
- XFEL crystallography reveals catalytic cycle dynamics during non-native substrate oxidation by cytochrome P450BM3.Communications chemistry · 2025Article
- Vibrational analyses of the reaction of oxymyoglobin with NO using a photolabile caged NO donor at cryogenic temperatures.Journal of inorganic biochemistry · 2024Article
- Article
- Real-time observation of a metal complex-driven reaction intermediate using a porous protein crystal and serial femtosecond crystallography.Nature communications · 2024Article
- Changes in an enzyme ensemble during catalysis observed by high-resolution XFEL crystallography.Science advances · 2024Article
- The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- The High-Pressure Freezing Laboratory for Macromolecular Crystallography (HPMX), an ancillary tool for the macromolecular crystallography beamlines at the ESRF.Acta crystallographica. Section D, Structural biology · 2024Article
- Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochromeScience advances · 2023Article
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Authors and funding
35 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Time-resolved serial femtosecond crystallography using an X-ray free electron laser (XFEL) in conjunction with a photosensitive caged-compound offers a crystallographic method to track enzymatic reactions. Here we demonstrate the application of this method using fungal NO reductase, a heme-containing enzyme, at room temperature. Twenty milliseconds after caged-NO photolysis, we identify a NO-bound form of the enzyme, which is an initial intermediate with a slightly bent Fe-N-O coordination geometry at a resolution of 2.1 Å. The NO geometry is compatible with those analyzed by XFEL-based cryo-crystallography and QM/MM calculations, indicating that we obtain an intact Fe
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