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Yudhajeet Basak1, Jae-Hun Jeoung1, Lilith Domnik1

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Summary
This summary is machine-generated.

Air exposure inactivates carbon monoxide dehydrogenases (CODHs) through a multistep process. Initial reversible steps involve ligand blocking at the nickel ion, followed by irreversible nickel loss and structural rearrangement.

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Area of Science:

  • Biochemistry and Enzymology
  • Bioinorganic Chemistry
  • Microbial Metabolism

Background:

  • Ni,Fe-containing carbon monoxide dehydrogenases (CODHs) are crucial enzymes in anaerobic microorganisms, catalyzing the reversible conversion of carbon dioxide to carbon monoxide.
  • CODHs are highly sensitive to oxygen, rapidly losing activity upon air exposure, a phenomenon whose underlying mechanisms remain poorly understood.

Purpose of the Study:

  • To elucidate the time-dependent structural changes occurring at the metal centers of CODH-II upon exposure to air.
  • To identify the specific steps and molecular events responsible for the inactivation of CODHs in the presence of oxygen.

Main Methods:

  • Analysis of time-dependent structural alterations in the metal centers of CODH-II induced by air exposure.
  • Investigation of the protective effect of cyanide ligand binding on the Ni ion against oxygen-induced decomposition.

Main Results:

  • CODH inactivation by air is a multistep process initiated by a reversible step where a Ni,Fe-bridging ligand (μ-sulfido or chlorido) blocks the Ni ion's open coordination site.
  • Stabilization of the cluster by cyanide at the Ni ion confirms oxygen attack at this site.
  • The irreversible phase involves nickel loss, iron ion rearrangement, and disappearance of sulfido ligands.

Conclusions:

  • The findings suggest a reversible reductive reactivation mechanism that protects CODHs from transient over-oxidation.
  • Understanding these inactivation pathways is critical for harnessing CODH activity in biotechnological applications.