Interaction of Staphylococcus aureus di-iron Repair of Iron Centers protein with the iron-sulfur cluster assembly SUF system.

ABSTRACT: Repair of Iron Centers (RIC) proteins are present in several pathogens, including Staphylococcus aureus, contributing to resistance to nitroxidative stress and virulence. In this work, we investigated the molecular mechanisms by which S. aureus RIC facilitates iron mobilization, through structural analyses and functional studies. EPR spectroscopy shows that S. aureus RIC contains an antiferromagnetically coupled di-iron site, undergoing two sequential monoelectronic transitions with a reduction potential of +185 mV. The protein exhibits a stronger affinity for Fe³⁺ and releases Fe²⁺ more readily, suggesting facilitated Fe²⁺ mobilization. The first crystallographic structure for this protein reveals that the di-iron center is embedded in a four-helix bundle

SUBMITTER: Lourenco FM 

PROVIDER: S-EPMC12720416 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature