The Elusive Mononitrosylated [Fe₄ S₄ ] Cluster in Three Redox States.

ABSTRACT: Iron-sulfur clusters are well-established targets in biological nitric oxide (NO) chemistry, but the key intermediate in these processes-a mononitrosylated [Fe₄ S₄ ] cluster-has not been fully characterized in a protein or a synthetic model thereof. Here, we report the synthesis of a three-member redox series of isostructural mononitrosylated [Fe₄ S₄ ] clusters. Mononitrosylation was achieved by binding NO to a 3 : 1 site-differentiated [Fe₄ S₄ ]⁺ cluster; subsequent oxidation and reduction afforded the other members of the series. All three clusters feature a local high-spin Fe³⁺ center antiferromagnetically coupled to ³ [NO]^- . The observation of an anionic NO ligand suggests tha

SUBMITTER: Kim Y 

PROVIDER: S-EPMC9669169 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature