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   https://doi.org/10.1021/acs.inorgchem.3c02652  

   Lawrence, Erick A.; Huai, Xudong; Kim, Dongwook; Avdeev, Maxim; Chen, Yu; Skorupskii, Grigorii; Miura, Akira; Ferrenti, Austin; Waibel, Moritz; Kawaguchi, Shogo; et al (November 2023, Inorganic Chemistry)
2. Facile Fabrication of Composite Ag/Fe ₃ O ₄ and Porous Fe ₃ O ₄ Nanorods Based on Oblique Angle Codeposition

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3. Reactivity of [Fe ₄ S ₄ ] Clusters toward C1 Substrates: Mechanism, Implications, and Potential Applications

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4. Characterization of a Nitrogenase Iron Protein Substituted with a Synthetic [Fe ₄ Se ₄ ] Cluster

   https://doi.org/10.1002/anie.202202271  

   Solomon, Joseph B.; Tanifuji, Kazuki; Lee, Chi Chung; Jasniewski, Andrew J.; Hedman, Britt; Hodgson, Keith O.; Hu, Yilin; Ribbe, Markus W. (March 2022, Angewandte Chemie International Edition)

   Abstract The Fe protein of nitrogenase plays multiple roles in substrate reduction and cluster maturation via its redox‐active [Fe₄S₄] cluster. Here we report the synthesis and characterization of a water‐soluble [Fe₄Se₄] cluster that is used to substitute the [Fe₄S₄] cluster of theAzotobacter vinelandiiFe protein (AvNifH). Biochemical, EPR and XAS/EXAFS analyses demonstrate the ability of the [Fe₄Se₄] cluster to adopt the super‐reduced, all‐ferrous state upon its incorporation intoAvNifH. Moreover, these studies reveal that the [Fe₄Se₄] cluster inAvNifH already assumes a partial all‐ferrous state ([Fe₄Se₄]⁰) in the presence of dithionite, where its [Fe₄S₄] counterpart inAvNifH exists solely in the reduced state ([Fe₄S₄]¹⁺). Such a discrepancy in the redox properties of theAvNifH‐associated [Fe₄Se₄] and [Fe₄S₄] clusters can be used to distinguish the differential redox requirements for the substrate reduction and cluster maturation of nitrogenase, pointing to the utility of chalcogen‐substituted FeS clusters in future mechanistic studies of nitrogenase catalysis and assembly. 

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5. Design of a Fe ₄ S ₄ cluster into the core of a de novo four‐helix bundle

   https://doi.org/10.1002/bab.2003  

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