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
Authors
- Maxime Laurans (ORCID: https://orcid.org/0000-0002-8145-5714)
- Philippe Schollhammer (ORCID: https://orcid.org/0000-0001-8161-7878)
Institutions
- 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)
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
Funders
- European Commission
- Centre National de la Recherche Scientifique
- Université de Bretagne Occidentale