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May 31, 2026Angewandte Chemie International EditionOpen Access

A Non‐Covalent 4Fe–4S/2Fe Interface in HydF Guides FeFe‐Hydrogenase Maturation

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Authors

GCGiorgio CasertaPCPrincess R. CabotajeAWArmel T. Waffo

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Overview

Randomized trial demonstrates the non-covalent binding of 2Fe subsite to 4Fe–4S cluster, suggesting new insights into hydrogenase synthesis.

Key Points

  • Investigate the role of the HydF maturase and its 4Fe–4S cluster in the maturation of [FeFe]-hydrogenases.
  • Comprehensive 57Fe nuclear resonance vibrational spectroscopy was employed.
  • Selective isotopic labeling was used to track non-covalent interactions.
  • Protein structure predictions and comparisons with previous studies were carried out.
  • The [2Fe] subsite binds adjacent to the [4Fe–4S] cluster without forming a covalent cyanide bridge, indicating electronic coupling.
  • Structural predictions align with earlier studies and confirm the role of the [4Fe–4S] cluster in biosynthesis.
  • Interactions with the lipoate cofactor support reactive component positioning for the [2Fe] precursor.

Cite This Study

Caserta et al. (2026) studied this question.

synapsesocial.com/papers/6a1bd2375783ba022b6fdadbhttps://doi.org/10.1002/anie.8078898
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