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

Malin Khalil1, Elizaveta Kobeleva1, Cornelius C M Bernitzky1

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Summary

Researchers studied how carbon monoxide (CO) detaches and reattaches to a [NiFe] model hydrogenase. This reveals a unique window to study hydrogen (H2) binding and activation at the enzyme's active site.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Spectroscopy

Background:

  • Hydrogenases are crucial metalloenzymes for splitting dihydrogen (H2), a clean fuel.
  • Carbon monoxide (CO) inhibits hydrogenase activity by binding to the active site.
  • Photolysis of CO can restore enzyme activity, enabling study of H2 binding.

Purpose of the Study:

  • To investigate the reversible photodissociation and rebinding dynamics of CO at the active site of a [NiFe] model hydrogenase.
  • To characterize the reaction dynamics following CO photolysis using advanced spectroscopic techniques.
  • To establish a temporal window for studying H2 binding and activation independent of mass transport limitations.

Main Methods:

  • UVpump-IRprobe spectroscopy with a multiple-probe configuration.
  • Time-resolved measurements spanning picosecond to millisecond timescales.
  • Study of CO ligand dynamics at the [NiFe] model hydrogenase active site.

Main Results:

  • Demonstrated reversible photodissociation and rebinding of CO ligand.
  • Observed a significant temporal gap between rapid CO dissociation and slow rebinding.
  • Enabled detailed investigation of H2 binding and activation dynamics.

Conclusions:

  • CO photolysis provides a method to access and study the active state of [NiFe] hydrogenase.
  • The identified temporal window is crucial for understanding H2 activation mechanisms.
  • This approach overcomes limitations of H2 mass transport in studying hydrogenase function.