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The pathogens possess efficient enzymes which are able to mitigate the toxicity of reactive oxygen species (ROS) produced by some antibiotics and the host immune cells. Among them, the bacterial peroxiredoxin alkyl hydroperoxide reductase C (AhpC) is able to decompose efficiently several kinds of hydroperoxides. To decompose their substrates AhpC use a reactive cysteine residue (peroxidatic cysteine\u2014Cys<jats:sub>P<\/jats:sub>) that together with two other polar residues (Thr\/Ser and Arg) comprise the catalytic triad of these enzymes and are involved in the substrate targeting\/stabilization to allow a bimolecular nucleophilic substitution (S<jats:sub>N<\/jats:sub>2) reaction. Additionally to the high efficiency the AhpC is very abundant in the cells and present virulent properties in some bacterial species. Despite the importance of AhpC in bacteria, few studies aimed at using natural compounds as inhibitors of this class of enzymes. Some natural products were identified as human isoforms, presenting as common characteristics a bulk hydrophobic moiety and an \u03b1, \u03b2-unsaturated carbonylic system able to perform a thiol-Michael reaction. In this work, we evaluated two chemically related natural products: 1,4-dihydroxy-2-(3\u2019,7\u2019-dimethyl-1\u2019-oxo-2\u2019<jats:italic>E<\/jats:italic>,6\u2019-octadienyl) benzene (<jats:bold>C1<\/jats:bold>) and 4-hydroxy-2-(3\u2019,7\u2019-dimethyl-1\u2019-oxo-2\u2019<jats:italic>E<\/jats:italic>,6\u2019-octadienyl) benzoic acid (<jats:bold>C2<\/jats:bold>), both were isolated from branches<jats:italic>Piper crassinervium<\/jats:italic>(Piperaceae), over the peroxidase activity of AhpC from<jats:italic>Pseudomonas aeruginosa<\/jats:italic>(PaAhpC) and<jats:italic>Staphylococcus epidermidis<\/jats:italic>(SeAhpC). By biochemical assays we show that although both compounds can perform the Michael addition reaction, only compound<jats:bold>C2<\/jats:bold>was able to inhibit the PaAhpC peroxidase activity but not SeAhpC, presenting IC<jats:sub>50<\/jats:sub>= 20.3 \u03bcM. SDS-PAGE analysis revealed that the compound was not able to perform a thiol-Michael addition, suggesting another inhibition behavior. Using computer-assisted simulations, we also show that an acidic group present in the structure of compound<jats:bold>C2<\/jats:bold>may be involved in the stabilization by polar interactions with the Thr and Arg residues from the catalytic triad and several apolar interactions with hydrophobic residues. Finally,<jats:bold>C2<\/jats:bold>was not able to interfere in the peroxidase activity of the isoform Prx2 from humans or even the thiol proteins of the Trx reducing system from<jats:italic>Escherichia coli<\/jats:italic>(EcTrx and EcTrxR), indicating specificity for<jats:italic>P<\/jats:italic>.<jats:italic>aeruginosa<\/jats:italic>AhpC.<\/jats:p>","DOI":"10.1371\/journal.pone.0281322","type":"journal-article","created":{"date-parts":[[2023,2,24]],"date-time":"2023-02-24T19:04:37Z","timestamp":1677265477000},"page":"e0281322","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":5,"title":["Exploring functional and structural features of chemically related natural prenylated hydroquinone and benzoic acid from Piper crassinervium (Piperaceae) on bacterial peroxiredoxin inhibition"],"prefix":"10.1371","volume":"18","author":[{"given":"Vitoria Isabela","family":"Montanhero Cabrera","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gabrielle","family":"do Nascimento Sividanes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Natalia Fernanda","family":"Quintiliano","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marcos","family":"Hikari Toyama","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jo\u00e3o Henrique","family":"Ghilardi Lago","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1192-7296","authenticated-orcid":true,"given":"Marcos Antonio","family":"de Oliveira","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2023,2,24]]},"reference":[{"issue":"20","key":"pone.0281322.ref001","doi-asserted-by":"crossref","first-page":"E2100","DOI":"10.1073\/pnas.1401876111","article-title":"Antibiotics induce redox-related physiological alterations as part of their lethality","volume":"111","author":"DJ Dwyer","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pone.0281322.ref002","doi-asserted-by":"crossref","first-page":"109023","DOI":"10.1016\/j.cbi.2020.109023","article-title":"The role of reactive oxygen species in the biological activity of antimicrobial agents: An updated mini review","volume":"320","author":"PL Lam","year":"2020","journal-title":"Chem Biol Interact"},{"key":"pone.0281322.ref003","doi-asserted-by":"crossref","first-page":"102075","DOI":"10.1016\/j.redox.2021.102075","article-title":"Peroxiredoxin AhpC1 protects 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