The first and second zinc finger domains from Poly-ADP-ribose polymerase 1 (PARP1) are modified by hydrogen sulfide

S was assessed using a UV-visible monitored 4-chloro-7-nitrobenzofurazan (NBF-Cl)/dimedone switch-tagging approach. Persulfidation for both PARP1 peptide constructs was observed under zinc-bound, oxygenated conditions. Superoxide intermediates were detected during the reaction using both dihydroethidine fluorescence and superoxide dismutase trapping. Together, these findings provide evidence that CCHC-type PARP ZFs can undergo persulfidation when Zn is bound and provide support for persulfidation being a general post-translational (PTM) modification for ZFs with different secondary structural elements.