A bioinspired hetero-binuclear iron–molybdenum complex supported by tridentate sulfur donors and its catalytic activity toward hydrazine disproportionation

A bioinspired thiolate-bridged iron-molybdenum complex was designed and synthesized, featuring structural motifs similar to those found in the {FeS<sub>3</sub>Mo} moiety of FeMoco. Spectroscopic and computational studies reveal that it contains a low-spin Fe<sup>II</sup> centre and a Mo<sup>IV</sup> centre with weak metal-metal bonding. Furthermore, it has been proven to be a good catalyst for hydrazine disproportionation.

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Publication Details

Journal
Dalton Transactions
Published
2025-01-01
DOI
https://doi.org/10.1039/d5dt01575h
Primary Topic
Metalloenzymes and iron-sulfur proteins
Type
article
Field-Weighted Citation Impact
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article

A bioinspired hetero-binuclear iron–molybdenum complex supported by tridentate sulfur donors and its catalytic activity toward hydrazine disproportionation

Ruifeng Du, Jingping Qü, Xu Xiang, Dawei Yang et al.
Dalton Transactions
Metalloenzymes and iron-sulfur proteins
article

A bioinspired hetero-binuclear iron–molybdenum complex supported by tridentate sulfur donors and its catalytic activity toward hydrazine disproportionation

Ruifeng Du, Jingping Qü, Xu Xiang, Dawei Yang, Baomin Wang, Luyang Sun
article en

Abstract

A bioinspired thiolate-bridged iron-molybdenum complex was designed and synthesized, featuring structural motifs similar to those found in the {FeS<sub>3</sub>Mo} moiety of FeMoco. Spectroscopic and computational studies reveal that it contains a low-spin Fe<sup>II</sup> centre and a Mo<sup>IV</sup> centre with weak metal-metal bonding. Furthermore, it has been proven to be a good catalyst for hydrazine disproportionation.

Dalton TransactionsVol. 54(39)
East China University of Science and Technology (CN), Dalian University of Technology (CN), Dalian University (CN)
Openalex Percentile: Top 84%
Metalloenzymes and iron-sulfur proteins
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