Involvement of thiolate ligands in binding substrates to Fe–S clusters
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
Inorganic Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2008/DT/B817353M
Reference32 articles.
1. Carbon Dioxide Activation at the Ni,Fe-Cluster of Anaerobic Carbon Monoxide Dehydrogenase
2. Aconitase as Iron−Sulfur Protein, Enzyme, and Iron-Regulatory Protein
3. Catalytic Reduction of Hydrazine to Ammonia by the VFe3S4 Cubanes. Further Evidence for the Direct Involvement of the Heterometal in the Reduction of Nitrogenase Substrates and Possible Relevance to the Vanadium Nitrogenases
4. Catalytic Reduction of Hydrazine to Ammonia with MoFe3S4−Polycarboxylate Clusters. Possible Relevance Regarding the Function of the Molybdenum-Coordinated Homocitrate in Nitrogenase
5. Catalytic Reduction of cis-Dimethyldiazene by the [MoFe3S4]3+ Clusters. The Four-Electron Reduction of a NN Bond by a Nitrogenase-Relevant Cluster and Implications for the Function of Nitrogenase
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1. Structural insight into halide-coordinated [Fe4S4XnY4−n]2− clusters (X, Y = Cl, Br, I) by XRD and Mössbauer spectroscopy;Dalton Transactions;2023
2. Halide coordinated homoleptic [Fe4S4X4]2−and heteroleptic [Fe4S4X2Y2]2−clusters (X, Y = Cl, Br, I)—alternative preparations, structural analogies and spectroscopic properties in solution and solid state;Dalton Transactions;2016
3. Binding Substrates to Synthetic Fe-S-Based Clusters and the Possible Relevance to Nitrogenases;Bioinspired Catalysis;2014-08-22
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