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February 26, 2026Physical Chemistry Chemical Physics4 citationsOpen Access

A Zundel Ion in the Catalytic Proton Transfer Pathway of FeFe-Hydrogenase

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LLLingling LiuMKMax A. KlamkeFAFederica Arrigoni

Key Points

  • This research investigates the role of a Zundel ion in the proton transfer pathway of [FeFe]-hydrogenases.
  • Examined the catalytic mechanisms of [FeFe]-hydrogenases.
  • Analyzed the interaction of protons and molecular hydrogen.
  • Investigated the structure of the active site cofactor.
  • Identified metalloenzymes as key players in proton transfer.
  • Showed that molecular hydrogen is interconverted effectively in the process.

Abstract

FeFe-hydrogenases are metalloenzymes that catalyze the interconversion of protons, electrons, and molecular hydrogen (H2). Their active site cofactor is constituted by a 4Fe-4S cluster (4FeH) and a diiron site (2FeH),...

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Cite This Study

Liu et al. (2026) studied this question.

synapsesocial.com/papers/699f95ba1bc9fecf3dab3d9dhttps://doi.org/10.1039/d5cp04267d
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Rapid in situ encapsulation of [NiFe]-hydrogenase into covalent organic frameworks for robust hydrogen oxidation and evolution2026
  2. 2The Key Role of Proton‐Responsive Groups in Electrochemical Hydrogen Evolution Reaction2024 · 1 citations
  3. 3Two‐Dimensional Infrared Spectroscopy Reveals the Presence of a Bridging CO Ligand in Two Catalytic Intermediates of [FeFe] Hydrogenase2026
  4. 4The H-cluster of [FeFe] Hydrogenases: Its Enzymatic Synthesis and Parallel Inorganic Semisynthesis2024 · 9 citations
  5. 5Final Stages in the Biosynthesis of the [FeFe]‐Hydrogenase Active Site2024