{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["147(35)"],"submitter":["Chen HY"],"pubmed_abstract":["Pathogenic <i>Staphylococcus aureus</i> endures bursts of host-derived reactive nitrogen species, yet the molecular defenses that enable this resilience have remained unclear. We now show that the previously enigmatic di-iron enzyme ScdA functions as a nitrite reductase, converting nitrite to nitric oxide (NO), and we elucidate the structural elements that support this activity. Using an integrative toolkit─X-ray crystallography, solution NMR, AlphaFold modeling, and pulsed EPR/DEER─we solved the full-length homodimeric structure of ScdA and identified a robust di-iron center that forms stable iron-nitrosyl intermediates. Targeted mutagenesis reveals that redox-active cysteines and dimerization state tune catalytic output, whereas steady-state kinetics confirm efficient nitrite-to-NO turno"],"journal":["Journal of the American Chemical Society"],"pagination":["31558-31569"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12412097"],"repository":["biostudies-literature"],"pubmed_title":["Structure and Nitrite Reductase Activity of the Di-iron Protein ScdA in &lt;i&gt;Staphylococcus aureus&lt;/i&gt;."],"pmcid":["PMC12412097"],"pubmed_authors":["Tsai RF","Hu NJ","Fan-Chiang HY","Wu CY","Liao WY","Sue SC","Lu YS","Kuo HW","Chen HY","Lo FC","Cheng YC","Yang WK","Chiang YW"],"additional_accession":[]},"is_claimable":false,"name":"Structure and Nitrite Reductase Activity of the Di-iron Protein ScdA in &lt;i&gt;Staphylococcus aureus&lt;/i&gt;.","description":"Pathogenic <i>Staphylococcus aureus</i> endures bursts of host-derived reactive nitrogen species, yet the molecular defenses that enable this resilience have remained unclear. We now show that the previously enigmatic di-iron enzyme ScdA functions as a nitrite reductase, converting nitrite to nitric oxide (NO), and we elucidate the structural elements that support this activity. Using an integrative toolkit─X-ray crystallography, solution NMR, AlphaFold modeling, and pulsed EPR/DEER─we solved the full-length homodimeric structure of ScdA and identified a robust di-iron center that forms stable iron-nitrosyl intermediates. Targeted mutagenesis reveals that redox-active cysteines and dimerization state tune catalytic output, whereas steady-state kinetics confirm efficient nitrite-to-NO turno","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-05-29T21:50:29.355Z","creation":"2026-04-08T06:08:12.273Z"},"accession":"S-EPMC12412097","cross_references":{"pubmed":["40846682"],"doi":["10.1021/jacs.5c05573"]}}