A Role for Two Conserved Arginine Residues in Protected Persulfide Transfer by SufE-Dependent SufS Cysteine Desulfurases.

ABSTRACT: Under stress conditions, iron-sulfur cluster biogenesis in Escherichia coli is initiated by the cysteine desulfurase, SufS, via the SUF pathway. SufS is a type II cysteine desulfurase that catalyzes the PLP-dependent breakage of an l-cysteine C-S bond to generate l-alanine and a covalent active site persulfide. The cysteine desulfurase activity of SufS is activated by SufE, which accepts the covalent persulfide from SufS to regenerate the active site. Based on analysis of the SufS/SufE structure, it was hypothesized that two conserved arginine residues in the SufS active site, R56 and R359, could be important for persulfide transfer from SufS to SufE by regulating the positioning of the α3-α4 loop on SufS. To investigate this hypothesis, site-directed mutagenesis was used to obtain

SUBMITTER: Gogar RK 

PROVIDER: S-EPMC12302911 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature