Journal Article PUBDB-2024-04984

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Structural Dynamics of Metalloproteins and Redox Enzymology with Mix-and-Inject Time-Resolved Serial Femtosecond Crystallography

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2024
ACS Washington, DC

ACS catalysis 14(14), 10853-10870 () [10.1021/acscatal.4c02526]
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Abstract: Time-resolved serial femtosecond crystallography (tr-SFX) enables the study of biomolecules in action at room temperature, thus facilitating the construction of in crystallo mini-3D biomolecular series (a stop-motion series) of biochemical reactions with unprecedented spatiotemporal details. One of the challenges encountered in expanding this method is the insufficient tools available for triggering the biomacromolecular reaction. Here, we highlight recent advances and challenges in the mix-and-inject (diffusion-based) tr-SFX (MISC) as a promising triggering method for studying the structural dynamics of metalloproteins, redox enzymes, and their reaction kinetics. We further discuss the results obtained using MISC tr-SFX and propose complex MISC (cMISC) as a tool to study complex reaction kinetics such as theenzyme-catalyzed bisubstrate (sequential and ping-pong) reactions.

Classification:

Contributing Institute(s):
  1. SPB/SFX (XFEL_E1_SPB/SFX)
Research Program(s):
  1. 6G13 - Accelerator of European XFEL (POF4-6G13) (POF4-6G13)
Experiment(s):
  1. Experiments at XFEL

Appears in the scientific report 2024
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Medline ; Creative Commons Attribution CC BY 4.0 ; OpenAccess ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Essential Science Indicators ; IF >= 10 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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 Record created 2024-07-05, last modified 2025-07-23


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