Exploring protonation sites with cation-responsive polyethylene glycol (PEG) tethers in [FeFe]-hydrogenase mimics

Na + and K + coordination influence protonation of [FeFe]H 2 ase mimics with polyether-linked triazoles. In TFA protonated triazoles avoid K + , boosting TOF, while Na + keeps coordination lowering activity. This insight aids in the design of HER catalysts.

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Publication Details

Journal
Inorganic Chemistry Frontiers
Published
2025-01-01
DOI
https://doi.org/10.1039/d5qi00170f
Citations
1
Primary Topic
Metalloenzymes and iron-sulfur proteins
Type
article
Field-Weighted Citation Impact
0.36

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article

Exploring protonation sites with cation-responsive polyethylene glycol (PEG) tethers in [FeFe]-hydrogenase mimics

Elena Sáez, Alba Collado, Miguel Á. Sierra, Alejandro Torres et al.
1 citations
Inorganic Chemistry Frontiers
Metalloenzymes and iron-sulfur proteins
0.36
article

Exploring protonation sites with cation-responsive polyethylene glycol (PEG) tethers in [FeFe]-hydrogenase mimics

Elena Sáez, Alba Collado, Miguel Á. Sierra, Alejandro Torres, Sergio Aguado
article en
1 citations

Abstract

Na + and K + coordination influence protonation of [FeFe]H 2 ase mimics with polyether-linked triazoles. In TFA protonated triazoles avoid K + , boosting TOF, while Na + keeps coordination lowering activity. This insight aids in the design of HER catalysts.

Inorganic Chemistry Frontiers
Universidad Complutense de Madrid (ES), Instituto de Química Orgánica General (ES), Universidad Autónoma de Madrid (ES)
Ministerio de Ciencia, Innovación y Universidades
Openalex Percentile: Top 45%
Metalloenzymes and iron-sulfur proteins
0.36
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