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Creators/Authors contains: "Tanifuji, Kazuki"

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  1. ; ; ; ; ; ; ; ; ; ; et al (, ChemBioChem)
    Accepted Manuscript Full Text Available
  2. ; ; ; ; ; ; (, JACS Au)
    null (Ed.)
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  3. ; ; ; ; ; ; (, Nature Catalysis)
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  4. ; ; ; ; ; ; ; (, 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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