Model of the MitoNEET [2Fe-2S] Cluster Shows Proton Coupled Electron Transfer.

ABSTRACT: MitoNEET is an outer membrane protein whose exact function remains unclear, though a role of this protein in redox and iron sensing as well as in controlling maximum mitochondrial respiratory rates has been discussed. It was shown to contain a redox active and acid labile [2Fe-2S] cluster which is ligated by one histidine and three cysteine residues. Herein we present the first synthetic analogue with biomimetic {SN/S₂} ligation which could be structurally characterized in its diferric form, 5^2-. In addition to being a high fidelity structural model for the biological cofactor, the complex is shown to mediate proton coupled electron transfer (PCET) at the {SN} ligated site, pointing at a potential functional role of the enzyme's unique His ligand. Full PCET thermodyna

SUBMITTER: Bergner M 

PROVIDER: S-EPMC5812485 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature