{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li J"],"funding":["Directorate for Biological Sciences","Directorate for Mathematical and Physical Sciences","Welch Foundation","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["e202407018"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11686441"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["63(49)"],"pubmed_abstract":["Bifunctional catalase-peroxidase (KatG) features a posttranslational methionine-tyrosine-tryptophan (MYW) crosslinked cofactor crucial for its catalase function, enabling pathogens to neutralize hydrogen peroxide during infection. We discovered the presence of indole nitrogen-linked hydroperoxyl adduct (MYW-OOH) in Mycobacterium tuberculosis KatG in the solution state under ambient conditions, suggesting its natural occurrence. By isolating predominantly MYW-OOH-containing KatG protein, we investigated the chemical stability and functional impact of MYW-OOH. We discovered that MYW-OOH inhibits catalase activity, presenting a unique temporary lock. Exposure to peroxide or increased temperature removes the hydroperoxyl adduct from the protein cofactor, converting MYW-OOH to MYW and restoring"],"journal":["Angewandte Chemie (International ed. in English)"],"pubmed_title":["Indole N-Linked Hydroperoxyl Adduct of Protein-Derived Cofactor Modulating Catalase-Peroxidase Functions."],"pmcid":["PMC11686441"],"funding_grant_id":["R01 GM152982","F31GM145187","CHE-2204225","AX-2110-20220331","F31 GM145187","R01GM108988","P30 GM133894","MCB-1616059","R01 GM108988","R01GM152982"],"pubmed_authors":["Davis I","Li J","Nguyen RC","Jarzecki AA","Goodwin DC","Duan R","Griffth WP","Liu A","Traore ES"],"additional_accession":[]},"is_claimable":false,"name":"Indole N-Linked Hydroperoxyl Adduct of Protein-Derived Cofactor Modulating Catalase-Peroxidase Functions.","description":"Bifunctional catalase-peroxidase (KatG) features a posttranslational methionine-tyrosine-tryptophan (MYW) crosslinked cofactor crucial for its catalase function, enabling pathogens to neutralize hydrogen peroxide during infection. We discovered the presence of indole nitrogen-linked hydroperoxyl adduct (MYW-OOH) in Mycobacterium tuberculosis KatG in the solution state under ambient conditions, suggesting its natural occurrence. By isolating predominantly MYW-OOH-containing KatG protein, we investigated the chemical stability and functional impact of MYW-OOH. We discovered that MYW-OOH inhibits catalase activity, presenting a unique temporary lock. Exposure to peroxide or increased temperature removes the hydroperoxyl adduct from the protein cofactor, converting MYW-OOH to MYW and restoring","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-05-29T11:37:01.003Z","creation":"2026-04-08T04:28:12.783Z"},"accession":"S-EPMC11686441","cross_references":{"pubmed":["39300819"],"doi":["10.1002/anie.202407018"]}}