Characterization of a mechanistic connection between persulfide transfer and ATP hydrolysis in the SufBC2D scaffold of the Suf Fe-S cluster assembly pathway.

ABSTRACT: The Suf pathway is the most common pathway for bacterial iron-sulfur cluster assembly and uses the SufBC2D complex as a scaffold for cluster formation. In most Gram-negative bacteria, the SufB subunit of SufBC2D accepts a persulfide from the transpersulfurase, SufE, for incorporation into nascent clusters. There is no reported structure for the SufBC2D-E complex and mechanistic details concerning the coordination of persulfide delivery with other SufBC2D activities are unclear. Using the Suf pathway from Escherichia coli as a model system, we report that SufE acts as a noncompetitive inhibitor of SufBC2D ATPase activity with a Ki value of 1.8 ± 0.2 µM. This value corresponds with a KD value of 1.6 ± 0.2 µM for SufE binding to the SufBC2D complex determined by fluorescence polarization. The

SUBMITTER: Chhikara N 

PROVIDER: S-EPMC12378399 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature