{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T14:18:05Z","timestamp":1791814685449,"version":"4.3.4"},"reference-count":65,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2024,5,1]],"date-time":"2024-05-01T00:00:00Z","timestamp":1714521600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,5,1]],"date-time":"2024-05-01T00:00:00Z","timestamp":1714521600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,3,7]],"date-time":"2024-03-07T00:00:00Z","timestamp":1709769600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35-GM130183"],"award-info":[{"award-number":["R35-GM130183"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["F32-GM144988"],"award-info":[{"award-number":["F32-GM144988"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007270","name":"University of Michigan","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007270","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006049","name":"Comisi\u00f3n Sectorial de Investigaci\u00f3n Cient\u00edfica","doi-asserted-by":"publisher","award":["U20B01"],"award-info":[{"award-number":["U20B01"]}],"id":[{"id":"10.13039\/501100006049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005363","name":"Universidad de Buenos Aires","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005363","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100016217","name":"Institut Pasteur de Montevideo","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100016217","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100024018","name":"Programa de Desarrollo de las Ciencias B\u00e1sicas","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100024018","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100013616","name":"American Society for Biochemistry and Molecular Biology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100013616","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2024,5]]},"DOI":"10.1016\/j.jbc.2024.107149","type":"journal-article","created":{"date-parts":[[2024,3,11]],"date-time":"2024-03-11T12:14:56Z","timestamp":1710159296000},"page":"107149","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":17,"title":["Acidity of persulfides and its modulation by the protein environments in sulfide quinone oxidoreductase and thiosulfate sulfurtransferase"],"prefix":"10.1016","volume":"300","author":[{"given":"Dayana","family":"Benchoam","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5777-4822","authenticated-orcid":false,"given":"Ernesto","family":"Cuevasanta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8697-9958","authenticated-orcid":false,"given":"Joseph V.","family":"Roman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5921-4906","authenticated-orcid":false,"given":"Ruma","family":"Banerjee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6911-3132","authenticated-orcid":false,"given":"Beatriz","family":"Alvarez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2024.107149_bib1","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0076-6879(87)43009-7","article-title":"Sulfane sulfur","volume":"143","author":"Wood","year":"1987","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jbc.2024.107149_bib2","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1089\/ars.2010.3678","article-title":"Mitochondria and sulfide: a very old story of poisoning, feeding, and signaling?","volume":"15","author":"Bouillaud","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.jbc.2024.107149_bib3","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1021\/acs.chemrev.7b00205","article-title":"Chemical biology of H2S signaling through persulfidation","volume":"118","author":"Filipovic","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jbc.2024.107149_bib4","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nchembio779","article-title":"Trafficking in persulfides: delivering sulfur in biosynthetic pathways","volume":"2","author":"Mueller","year":"2006","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2024.107149_bib5","doi-asserted-by":"crossref","first-page":"26866","DOI":"10.1074\/jbc.M115.672816","article-title":"Reaction of hydrogen sulfide with disulfide and sulfenic acid to form the strongly nucleophilic persulfide","volume":"290","author":"Cuevasanta","year":"2015","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib6","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1089\/ars.2012.5041","article-title":"Polysulfides link H2S to protein thiol oxidation","volume":"19","author":"Greiner","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.jbc.2024.107149_bib7","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1002\/anie.201305876","article-title":"Detection of protein S-sulfhydration by a tag-switch technique","volume":"53","author":"Zhang","year":"2014","journal-title":"Angew. Chem. Int. Ed Engl."},{"key":"10.1016\/j.jbc.2024.107149_bib8","doi-asserted-by":"crossref","first-page":"20002","DOI":"10.1074\/jbc.M113.466177","article-title":"Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase","volume":"288","author":"Yadav","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib9","doi-asserted-by":"crossref","first-page":"7606","DOI":"10.1073\/pnas.1321232111","article-title":"Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling","volume":"111","author":"Ida","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2024.107149_bib10","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1021\/jacs.5b10494","article-title":"Biosynthesis and reactivity of cysteine persulfides in signaling","volume":"138","author":"Yadav","year":"2016","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2024.107149_bib11","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.aax8358","article-title":"Control of protein function through oxidation and reduction of persulfidated states","volume":"6","author":"D\u00f3ka","year":"2020","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2024.107149_bib12","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.1500968","article-title":"A\u00a0novel persulfide detection method reveals protein persulfide- and polysulfide-reducing functions of thioredoxin and glutathione systems","volume":"2","author":"D\u00f3ka","year":"2016","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2024.107149_bib13","doi-asserted-by":"crossref","first-page":"15466","DOI":"10.1074\/jbc.RA120.014728","article-title":"Acidity and nucleophilic reactivity of glutathione persulfide","volume":"295","author":"Benchoam","year":"2020","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib14","doi-asserted-by":"crossref","first-page":"6484","DOI":"10.1021\/jacs.7b02571","article-title":"Hydropersulfides: H-atom transfer agents par excellence","volume":"139","author":"Chauvin","year":"2017","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2024.107149_bib15","doi-asserted-by":"crossref","first-page":"387","DOI":"10.3109\/10715769409145638","article-title":"Free-radical repair by a novel perthiol: reversible hydrogen transfer and perthiyl radical formation","volume":"20","author":"Everett","year":"1994","journal-title":"Free Radic. Res."},{"key":"10.1016\/j.jbc.2024.107149_bib16","doi-asserted-by":"crossref","first-page":"6113","DOI":"10.1021\/bi500389m","article-title":"Deconstructing the catalytic efficiency of peroxiredoxin-5 peroxidatic cysteine","volume":"53","author":"Portillo-Ledesma","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2024.107149_bib17","doi-asserted-by":"crossref","first-page":"1778","DOI":"10.1021\/ja01492a058","article-title":"Reactivity of nucleophilic reagents toward esters","volume":"82","author":"Jencks","year":"1960","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2024.107149_bib18","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1021\/ja00860a005","article-title":"The factors determining nucleophilic reactivities","volume":"84","author":"Edwards","year":"1962","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2024.107149_bib19","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.freeradbiomed.2023.07.006","article-title":"Disulfides form persulfides at alkaline pH leading to potential overestimations in the cold cyanolysis method","volume":"207","author":"Benchoam","year":"2023","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.jbc.2024.107149_bib20","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1002\/cbic.202000661","article-title":"Hydrogen sulfide oxidation by sulfide quinone oxidoreductase","volume":"22","author":"Landry","year":"2021","journal-title":"Chembiochem"},{"key":"10.1016\/j.jbc.2024.107149_bib21","doi-asserted-by":"crossref","first-page":"1515","DOI":"10.1016\/j.chembiol.2019.09.010","article-title":"A\u00a0catalytic trisulfide in human sulfide quinone oxidoreductase catalyzes coenzyme A persulfide synthesis and inhibits butyrate oxidation","volume":"26","author":"Landry","year":"2019","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.jbc.2024.107149_bib22","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1016\/j.str.2019.03.002","article-title":"X-Ray structure of human sulfide:quinone oxidoreductase: Insights into the mechanism of mitochondrial hydrogen sulfide oxidation","volume":"27","author":"Jackson","year":"2019","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2024.107149_bib23","doi-asserted-by":"crossref","first-page":"3352","DOI":"10.1111\/j.1742-4658.2008.06482.x","article-title":"Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria","volume":"275","author":"Hildebrandt","year":"2008","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2024.107149_bib24","doi-asserted-by":"crossref","first-page":"30901","DOI":"10.1074\/jbc.M114.602664","article-title":"Organization of the human mitochondrial hydrogen sulfide oxidation pathway","volume":"289","author":"Libiad","year":"2014","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib25","doi-asserted-by":"crossref","first-page":"6804","DOI":"10.1021\/bi300778t","article-title":"Human sulfide:quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite","volume":"51","author":"Jackson","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2024.107149_bib26","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1021\/acschembio.8b00258","article-title":"Modulation of catalytic promiscuity during hydrogen sulfide oxidation","volume":"13","author":"Landry","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.jbc.2024.107149_bib27","doi-asserted-by":"crossref","first-page":"11641","DOI":"10.1074\/jbc.M117.788547","article-title":"H2S oxidation by nanodisc-embedded human sulfide quinone oxidoreductase","volume":"292","author":"Landry","year":"2017","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib28","doi-asserted-by":"crossref","first-page":"44561","DOI":"10.1074\/jbc.M112.407411","article-title":"Characterization of patient mutations in human persulfide dioxygenase (ETHE1) involved in H2S catabolism","volume":"287","author":"Kabil","year":"2012","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib29","doi-asserted-by":"crossref","first-page":"4739","DOI":"10.1021\/bi500650h","article-title":"Biosynthesis of a central intermediate in hydrogen sulfide metabolism by a novel human sulfurtransferase and its yeast ortholog","volume":"53","author":"Melideo","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2024.107149_bib30","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1016\/S0021-9258(19)42997-9","article-title":"An Expanded mechanism for rhodanese catalysis","volume":"249","author":"Schlesinger","year":"1974","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib31","doi-asserted-by":"crossref","first-page":"3233","DOI":"10.1021\/bi00713a006","article-title":"Human liver rhodanese. Nonlinear kinetic behavior in a double displacement mechanism","volume":"13","author":"Jarabak","year":"1974","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2024.107149_bib32","series-title":"Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding","first-page":"110","article-title":"The meaning of kcat\/KM: the specificity constant (Chapter 3: the basic equations of enzyme kinetics)","author":"Fersht","year":"1999"},{"key":"10.1016\/j.jbc.2024.107149_bib33","doi-asserted-by":"crossref","first-page":"2556","DOI":"10.1021\/acs.jchemed.1c01268","article-title":"Visual interpretation of the meaning of kcat\/KM in enzyme kinetics","volume":"99","author":"Park","year":"2022","journal-title":"J.\u00a0Chem. Educ."},{"key":"10.1016\/j.jbc.2024.107149_bib34","doi-asserted-by":"crossref","first-page":"1799","DOI":"10.1021\/j100255a052","article-title":"The second dissociation constant of sulfur dioxide.water","volume":"89","author":"Rhee","year":"1985","journal-title":"J.\u00a0Phys. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib35","first-page":"185","article-title":"Dissociation constant of hydrogen cyanide in saline solutions","volume":"7","author":"Verhoeven","year":"1990","journal-title":"Min. Metall. Explor."},{"key":"10.1016\/j.jbc.2024.107149_bib36","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/s10498-019-09361-y","article-title":"Kinetics of thiocyanate formation by reaction of cyanide and its Iron complexes with thiosulfate","volume":"25","author":"Kurashova","year":"2019","journal-title":"Aquat. Geochem."},{"key":"10.1016\/j.jbc.2024.107149_bib37","doi-asserted-by":"crossref","first-page":"7894","DOI":"10.1016\/S0021-9258(20)81997-8","article-title":"The use of intrinsic protein fluorescence to quantitate enzyme-bound persulfide and to measure equilibria between intermediates in rhodanese catalysis","volume":"258","author":"Horowitz","year":"1983","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib38","doi-asserted-by":"crossref","first-page":"7319","DOI":"10.1021\/bi00371a012","article-title":"Active site modifications quench intrinsic fluorescence of rhodanese by different mechanisms","volume":"25","author":"Cannella","year":"1986","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2024.107149_bib39","doi-asserted-by":"crossref","first-page":"8109","DOI":"10.1016\/S0021-9258(17)34369-7","article-title":"Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal","volume":"253","author":"Weng","year":"1978","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib40","doi-asserted-by":"crossref","first-page":"2049","DOI":"10.1021\/acscatal.7b02432","article-title":"Unraveling the mechanism of cysteine persulfide formation catalyzed by 3-mercaptopyruvate sulfurtransferases","volume":"8","author":"Lec","year":"2018","journal-title":"ACS Catal."},{"key":"10.1016\/j.jbc.2024.107149_bib41","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.jpba.2014.02.023","article-title":"The species- and site-specific acid\u2013base properties of biological thiols and their homodisulfides","volume":"95","author":"Mirzahosseini","year":"2014","journal-title":"J.\u00a0Pharm. Biomed. Anal."},{"key":"10.1016\/j.jbc.2024.107149_bib42","doi-asserted-by":"crossref","first-page":"2797","DOI":"10.1021\/ja00790a009","article-title":"Nuclear magnetic resonance studies of the acid-base chemistry of amino acids and peptides. I. Microscopic ionization constants of glutathione and methylmercury-complexed glutathione","volume":"95","author":"Rabenstein","year":"1973","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2024.107149_bib43","doi-asserted-by":"crossref","first-page":"6227","DOI":"10.1021\/ja00752a039","article-title":"Equilibria for the reaction of cysteine and derivatives with formaldehyde and protons","volume":"93","author":"Kallen","year":"1971","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2024.107149_bib44","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.ab.2012.12.017","article-title":"Determination of acidity and nucleophilicity in thiols by reaction with monobromobimane and fluorescence detection","volume":"435","author":"Sardi","year":"2013","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jbc.2024.107149_bib45","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1039\/P29900001421","article-title":"Relative nucleophilicities of aryldisulphide and thiolate ions in dimethylacetamide estimated from their reaction rates with alkyl halides","volume":"2","author":"Bena\u00efchouche","year":"1990","journal-title":"J.\u00a0Chem. Soc. Perkin Trans."},{"key":"10.1016\/j.jbc.2024.107149_bib46","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1002\/etc.5620071108","article-title":"Some reactions of naturally occurring nucleophiles with haloalkanes in water","volume":"7","author":"Haag","year":"1988","journal-title":"Environ. Toxicol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib47","doi-asserted-by":"crossref","first-page":"20630","DOI":"10.1021\/jacs.2c07380","article-title":"Sulfane decreases the nucleophilic reactivity of zinc thiolates: Implications for biological reactive sulfur species","volume":"144","author":"Seo","year":"2022","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2024.107149_bib48","doi-asserted-by":"crossref","first-page":"13593","DOI":"10.1074\/jbc.RA119.008883","article-title":"Kinetics of formation and reactivity of the persulfide in the one-cysteine peroxiredoxin from Mycobacterium tuberculosis","volume":"294","author":"Cuevasanta","year":"2019","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib49","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1021\/ol0526930","article-title":"The alpha-effect in gas-phase SN2 reactions revisited","volume":"8","author":"Ren","year":"2006","journal-title":"Org. Lett."},{"key":"10.1016\/j.jbc.2024.107149_bib50","doi-asserted-by":"crossref","first-page":"20840","DOI":"10.1002\/anie.202106053","article-title":"Origin of the \u03b1-effect in SN2 reactions","volume":"60","author":"Hansen","year":"2021","journal-title":"Angew. Chem. Int. Ed Engl."},{"key":"10.1016\/j.jbc.2024.107149_bib51","doi-asserted-by":"crossref","first-page":"3545","DOI":"10.1021\/jo00139a033","article-title":"The \u03b1 effect: on the origin of transition-state stabilization","volume":"47","author":"Hoz","year":"1982","journal-title":"J.\u00a0Org. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib52","doi-asserted-by":"crossref","first-page":"7801","DOI":"10.1016\/j.tet.2004.05.006","article-title":"The \u03b1-effect and its modulation by solvent","volume":"60","author":"Buncel","year":"2004","journal-title":"Tetrahedron"},{"key":"10.1016\/j.jbc.2024.107149_bib53","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/j.bbrc.2015.02.128","article-title":"Chloride concentrations in human hepatic cytosol and mitochondria are a function of age","volume":"459","author":"Jahn","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2024.107149_bib54","article-title":"Thiosulfate Mediates Cytoprotective effects of hydrogen sulfide against Neuronal Ischemia","volume":"4","author":"Marutani","year":"2015","journal-title":"J.\u00a0Am. Heart Assoc."},{"key":"10.1016\/j.jbc.2024.107149_bib55","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1038\/nm.1907","article-title":"Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy","volume":"15","author":"Tiranti","year":"2009","journal-title":"Nat. Med."},{"key":"10.1016\/j.jbc.2024.107149_bib56","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1080\/15216540211468","article-title":"Structural basis of perturbed pKa values of catalytic groups in enzyme active sites","volume":"53","author":"Harris","year":"2002","journal-title":"IUBMB Life"},{"key":"10.1016\/j.jbc.2024.107149_bib57","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/0022-2836(79)90236-5","article-title":"The structure of bovine liver rhodanese. II. The active site in the sulfur-substituted and the sulfur-free enzyme","volume":"127","author":"Ploegman","year":"1979","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2024.107149_bib58","doi-asserted-by":"crossref","first-page":"13938","DOI":"10.1074\/jbc.274.20.13938","article-title":"NH2-terminal sequence Truncation decreases the stability of bovine rhodanese, minimally Perturbs its crystal structure, and Enhances Interaction with GroEL under Native conditions","volume":"274","author":"Trevino","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib59","doi-asserted-by":"crossref","first-page":"8220","DOI":"10.1016\/S0021-9258(17)37182-X","article-title":"The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249","volume":"269","author":"Luo","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107149_bib60","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/0076-6879(95)51117-2","article-title":"Bromobimane probes for thiols","volume":"251","author":"Kosower","year":"1995","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jbc.2024.107149_bib61","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/S0076-6879(82)87025-0","article-title":"Buffers of constant ionic strength for studying pH-dependent processes","volume":"87","author":"Ellis","year":"1982","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jbc.2024.107149_bib62","series-title":"The Proteomics Protocols Handbook","first-page":"571","article-title":"Protein Identification and analysis Tools on the ExPASy Server","author":"Gasteiger","year":"2005"},{"key":"10.1016\/j.jbc.2024.107149_bib63","series-title":"NIST Standard Reference Database","article-title":"NIST Critical stability constants of metal complexes database","author":"Smith","year":"1993"},{"key":"10.1016\/j.jbc.2024.107149_bib64","series-title":"Ionisation Constants of Organic Acids in Aqueous Solution","author":"Serjeant","year":"1979"},{"key":"10.1016\/j.jbc.2024.107149_bib65","doi-asserted-by":"crossref","first-page":"W431","DOI":"10.1093\/nar\/gkab314","article-title":"Mol\u2217 Viewer: modern web app for 3D visualization and analysis of large biomolecular structures","volume":"49","author":"Sehnal","year":"2021","journal-title":"Nucleic Acids Res."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824016442?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824016442?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T20:55:55Z","timestamp":1777409755000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925824016442"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,5]]},"references-count":65,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2024,5]]}},"alternative-id":["S0021925824016442"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2024.107149","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2024,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Acidity of persulfides and its modulation by the protein environments in sulfide quinone oxidoreductase and thiosulfate sulfurtransferase","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2024.107149","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"107149"}}