Bioinspired bi- or trinuclear FeMoS model complexes for the partial region of FeMo cofactor of nitrogenase

Sulfur-rich {FeMo} complexes of low nuclearity ({Fe 2 Mo}, {FeMo}) can be considered as simple truncated models of the cofactor of Mo‑nitrogenase. They are suitable to address questions concerning the role of the still unclear FeMo cooperativity in the biological N 2 -reduction process performed by this metallo-enzyme. This review affords a state of the art of the chemistry of di- and tri-heterometallic {FeMoS} complexes. Although well-defined synthetic procedures have been evidenced for the design of such compounds, very few investigations on their activity towards N 2 and related substrates have been reported. This shows the interest to develop new light bio-inspired {FeMoS} molecules and to study their reactivity, as well as their redox behaviours, to help to better understand the biological N 2 -fixation. This approach involving di- and tri- heterometallic {FeMoS} species is a promising field of investigation. • Sulfur-rich {FeMo}-complexes of low nuclearity ({Fe 2 Mo}, {FeMo}) can be simple truncated models of the cofactor of [FeMo]-nitrogenase • The chemistry of {FeMo} compounds will lead to novel insights into understanding the functioning of the nitrogenase cofactor • The activity of {FeMo} derivatives towards N 2 and related substrates remains to be developed • Bioinspired {FeMo] complexes offer underdeveloped perspectives for the activation of small molecules

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Publication Details

Journal
Coordination Chemistry Reviews
Published
2025-09-16
DOI
https://doi.org/10.1016/j.ccr.2025.217128
Primary Topic
Metalloenzymes and iron-sulfur proteins
Type
article
Field-Weighted Citation Impact
0.00

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article

Bioinspired bi- or trinuclear FeMoS model complexes for the partial region of FeMo cofactor of nitrogenase

Maxime Laurans, Philippe Schollhammer
Coordination Chemistry Reviews
Metalloenzymes and iron-sulfur proteins
article

Bioinspired bi- or trinuclear FeMoS model complexes for the partial region of FeMo cofactor of nitrogenase

Maxime Laurans, Philippe Schollhammer
article en

Abstract

Sulfur-rich {FeMo} complexes of low nuclearity ({Fe 2 Mo}, {FeMo}) can be considered as simple truncated models of the cofactor of Mo‑nitrogenase. They are suitable to address questions concerning the role of the still unclear FeMo cooperativity in the biological N 2 -reduction process performed by this metallo-enzyme. This review affords a state of the art of the chemistry of di- and tri-heterometallic {FeMoS} complexes. Although well-defined synthetic procedures have been evidenced for the design of such compounds, very few investigations on their activity towards N 2 and related substrates have been reported. This shows the interest to develop new light bio-inspired {FeMoS} molecules and to study their reactivity, as well as their redox behaviours, to help to better understand the biological N 2 -fixation. This approach involving di- and tri- heterometallic {FeMoS} species is a promising field of investigation. • Sulfur-rich {FeMo}-complexes of low nuclearity ({Fe 2 Mo}, {FeMo}) can be simple truncated models of the cofactor of [FeMo]-nitrogenase • The chemistry of {FeMo} compounds will lead to novel insights into understanding the functioning of the nitrogenase cofactor • The activity of {FeMo} derivatives towards N 2 and related substrates remains to be developed • Bioinspired {FeMo] complexes offer underdeveloped perspectives for the activation of small molecules

Coordination Chemistry ReviewsVol. 548
Centre National de la Recherche Scientifique (FR), Université de Bretagne Occidentale (FR), Université de Versailles Saint-Quentin-en-Yvelines (FR), Université Paris-Saclay (FR), Laboratoire Chimie Electrochimie Moléculaires et Chimie Analytique (FR), Institut Lavoisier de Versailles (FR)
European Commission, Centre National de la Recherche Scientifique, Université de Bretagne Occidentale
Openalex Percentile: Top 84%
Metalloenzymes and iron-sulfur proteins
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