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June 21, 2026Inorganic ChemistryOpen Access

From Carbon-Monoxide Inhibition to Light Activation: Probing NiFe Hydrogenase Dynamics by Multiscale Time-Resolved Infrared Spectroscopy

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Authors

MKMalin KhalilEKElizaveta KobelevaCBCornelius C. M. Bernitzky

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Overview

Multiscale time-resolved infrared spectroscopy reveals hydrogenase dynamics through carbon-monoxide inhibition and light activation.

Key Points

  • The study aims to explore the dynamics of [NiFe] hydrogenases using time-resolved infrared spectroscopy.
  • Utilized multiscale time-resolved infrared spectroscopy to investigate hydrogenase behavior.
  • Examined the effects of carbon-monoxide inhibition and light activation on enzyme dynamics.
  • Demonstrated that carbon-monoxide inhibition alters the structural dynamics of hydrogenases.
  • Showed that light activation leads to distinct changes in enzyme behavior.
  • Revealed specific molecular mechanisms governing hydrogenase activity under different conditions.

Cite This Study

Khalil et al. (2026) studied this question.

synapsesocial.com/papers/6a377edf24f042ddf4c59c1bhttps://doi.org/10.1021/acs.inorgchem.6c01321
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