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March 29, 2026The Journal of Physical Chemistry LettersOpen Access

Photoactivation of FeFe Hydrogenase Studied by Multiscale Time-Resolved Infrared Spectroscopy

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Authors

EKElizaveta KobelevaMKMalin KhalilMLManon T. Lachmann

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Overview

Multiscale spectroscopy reveals photochemical activation mechanisms in [FeFe] hydrogenase, suggesting new insights for catalysis.

Key Points

  • The research aims to elucidate the catalytic mechanism of [FeFe] hydrogenases through time-resolved spectroscopy.
  • Utilized multiscale UV-pump-IR-probe spectroscopy
  • Studied the reversible activation of the CO-inhibited Hox-CO state
  • Conducted experiments over picosecond to millisecond time scales
  • Analyzed the dissociation of the extrinsic CO during photolysis
  • CO dissociates from Hox-CO in picoseconds
  • Hox state remains unbound for up to milliseconds
  • Enzyme becomes available for H2 binding during this time
  • The approach allows real-time observation of catalytic processes

Cite This Study

Kobeleva et al. (2026) studied this question.

synapsesocial.com/papers/69c8c2fcde0f0f753b39d828https://doi.org/10.1021/acs.jpclett.6c00408
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