{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T06:43:58Z","timestamp":1793083438988,"version":"4.5.0"},"reference-count":61,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100021778","name":"Agencia Nacional de Promoci\u00f3n de la Investigaci\u00f3n, el Desarrollo Tecnol\u00f3gico y la Innovaci\u00f3n","doi-asserted-by":"publisher","award":["PICT 2018 \\u2013 00794"],"award-info":[{"award-number":["PICT 2018 \\u2013 00794"]}],"id":[{"id":"10.13039\/501100021778","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007351","name":"University of Buenos Aires Secretariat of Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100007351","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\/501100010253","name":"Secretar\u00eda de Ciencia y T\u00e9cnica, Universidad de Buenos Aires","doi-asserted-by":"publisher","award":["2023 20020220200002BA"],"award-info":[{"award-number":["2023 20020220200002BA"]}],"id":[{"id":"10.13039\/501100010253","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002923","name":"Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas","doi-asserted-by":"publisher","award":["PIP 21-23 GI 11220200102757CO"],"award-info":[{"award-number":["PIP 21-23 GI 11220200102757CO"]}],"id":[{"id":"10.13039\/501100002923","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2025,2]]},"DOI":"10.1016\/j.bbrc.2025.151319","type":"journal-article","created":{"date-parts":[[2025,1,10]],"date-time":"2025-01-10T02:31:46Z","timestamp":1736476306000},"page":"151319","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"special_numbering":"C","title":["Coordination of inorganic disulfide species to ferric N-acetyl microperoxidase 11"],"prefix":"10.1016","volume":"748","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0721-5982","authenticated-orcid":false,"given":"Jonathan Alexis","family":"C\u00f3rdova","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9528-8275","authenticated-orcid":false,"given":"Juan Cruz","family":"Palermo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1604-6196","authenticated-orcid":false,"given":"Sara E.","family":"Bari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3794-5713","authenticated-orcid":false,"given":"Luciana","family":"Capece","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2025.151319_bib1","doi-asserted-by":"crossref","first-page":"3279","DOI":"10.1039\/C8CS00826D","article-title":"The role of polysulfide dianions and radical anions in the chemical, physical and biological sciences, including sulfur-based batteries","volume":"48","author":"Steudel","year":"2019","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.bbrc.2025.151319_bib2","doi-asserted-by":"crossref","first-page":"131","DOI":"10.2183\/pjab.91.131","article-title":"Hydrogen sulfide and polysulfides as signaling molecules","volume":"91","author":"Kimura","year":"2015","journal-title":"Proc. Jpn. Acad. Ser. B Phys. Biol. Sci."},{"key":"10.1016\/j.bbrc.2025.151319_bib3","first-page":"7878","article-title":"Hemeproteins AS targets for sulfide species","author":"Boubeta","year":"2019","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.bbrc.2025.151319_bib4","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2023.102617","article-title":"Interactions of reactive sulfur species with metalloproteins","volume":"60","author":"Dom\u00e1n","year":"2023","journal-title":"Redox Biol."},{"key":"10.1016\/j.bbrc.2025.151319_bib5","doi-asserted-by":"crossref","first-page":"5584","DOI":"10.1074\/jbc.M117.774943","article-title":"Structural and mechanistic insights into hemoglobin-catalyzed hydrogen sulfide oxidation and the fate of polysulfide products","volume":"292","author":"Vitvitsky","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib6","doi-asserted-by":"crossref","first-page":"2300","DOI":"10.1021\/acschembio.8b00463","article-title":"Cytochrome c reduction by H 2 S potentiates sulfide signaling","volume":"13","author":"Vitvitsky","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.bbrc.2025.151319_bib7","doi-asserted-by":"crossref","first-page":"15288","DOI":"10.1021\/jacs.9b07338","article-title":"Potent activation of indoleamine 2,3-dioxygenase by polysulfides","volume":"141","author":"Nelp","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbrc.2025.151319_bib8","article-title":"Reduction of metmyoglobin by inorganic disulfide species","author":"Palermo","year":"2023","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbrc.2025.151319_bib9","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2023.112313","article-title":"Binding mechanism of disulfide species to ferric hemeproteins: the case of metmyoglobin","volume":"247","author":"C\u00f3rdova","year":"2023","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbrc.2025.151319_bib10","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/S1570-9639(03)00044-X","article-title":"Reaction mechanism and regulation of cystathionine \u03b2-synthase","volume":"1647","author":"Banerjee","year":"2003","journal-title":"Biochim. Biophys. Acta Protein Proteonomics"},{"key":"10.1016\/j.bbrc.2025.151319_bib11","doi-asserted-by":"crossref","first-page":"22457","DOI":"10.1074\/jbc.M109.010868","article-title":"Relative contributions of cystathionine \u03b2-synthase and \u03b3-cystathionase to H 2 S biogenesis via alternative trans-sulfuration reactions","volume":"284","author":"Singh","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib12","doi-asserted-by":"crossref","first-page":"85","DOI":"10.2174\/187152811794776286","article-title":"Hydrogen sulfide generation in mammals: the molecular biology of cystathionine-\u03b2-synthase (CBS) and cystathionine-\u03b3-lyase (CSE)","volume":"10","author":"Renga","year":"2011","journal-title":"IADT"},{"key":"10.1016\/j.bbrc.2025.151319_bib13","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-11004-7","article-title":"3-Mercaptopyruvate sulfurtransferase produces potential redox regulators cysteine- and glutathione-persulfide (Cys-SSH and GSSH) together with signaling molecules H2S2, H2S3 and H2S","volume":"7","author":"Kimura","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbrc.2025.151319_bib14","series-title":"Sulfurtransferases","first-page":"83","article-title":"3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide (H2S), polysulfides (H2Sn), and other S-sulfurated signaling molecules","author":"Kimura","year":"2023"},{"key":"10.1016\/j.bbrc.2025.151319_bib15","doi-asserted-by":"crossref","DOI":"10.1038\/srep14774","article-title":"Identification of H2S3 and H2S produced by 3-mercaptopyruvate sulfurtransferase in the brain","volume":"5","author":"Kimura","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbrc.2025.151319_bib16","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.bbrc.2025.151319_bib17","doi-asserted-by":"crossref","first-page":"9625","DOI":"10.1073\/pnas.0904165106","article-title":"The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration","volume":"106","author":"Marcia","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.bbrc.2025.151319_bib18","doi-asserted-by":"crossref","first-page":"896","DOI":"10.3390\/biom11060896","article-title":"Hydrogen sulfide (H2S) and polysulfide (H2Sn) signaling: the first 25 years","volume":"11","author":"Kimura","year":"2021","journal-title":"Biomolecules"},{"key":"10.1016\/j.bbrc.2025.151319_bib19","doi-asserted-by":"crossref","DOI":"10.1021\/acs.inorgchem.3c00593","article-title":"Autocatalytic mechanism in the anaerobic reduction of metmyoglobin by sulfide species","author":"Palermo","year":"2023","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib20","doi-asserted-by":"crossref","first-page":"7591","DOI":"10.1021\/acs.inorgchem.8b00478","article-title":"Mechanism of sulfide binding by ferric hemeproteins","volume":"57","author":"Boubeta","year":"2018","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib21","doi-asserted-by":"crossref","DOI":"10.1088\/2516-1075\/aca945","article-title":"Computational evaluation of relevant species in inorganic sulfur biochemistry","author":"Palermo","year":"2022","journal-title":"Electron. Struct"},{"key":"10.1016\/j.bbrc.2025.151319_bib22","doi-asserted-by":"crossref","first-page":"3165","DOI":"10.1021\/cr000055j","article-title":"Peptide-based Heme\u2212Protein models","volume":"101","author":"Lombardi","year":"2001","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bbrc.2025.151319_bib23","doi-asserted-by":"crossref","first-page":"4371","DOI":"10.1039\/b710940g","article-title":"Insights into porphyrin chemistry provided by the microperoxidases, the haempeptides derived from cytochrome c","author":"Marques","year":"2007","journal-title":"Dalton Trans."},{"key":"10.1016\/j.bbrc.2025.151319_bib24","doi-asserted-by":"crossref","first-page":"6885","DOI":"10.1021\/ic960434o","article-title":"Characterization of N-acetylated heme undecapeptide and some of its derivatives in aqueous media: monomeric model systems for hemoproteins","volume":"35","author":"Carraway","year":"1996","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib25","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/0162-0134(95)00026-7","article-title":"Monomeric ferric heme peptide derivatives: model systems for hemoproteins","volume":"60","author":"Carraway","year":"1995","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbrc.2025.151319_bib26","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1021\/ic502294z","article-title":"Reactivity of inorganic sulfide species toward a heme protein model","volume":"54","author":"Bieza","year":"2015","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib27","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1038\/336265a0","article-title":"The role of the distal histidine in myoglobin and haemoglobin","volume":"336","author":"Olson","year":"1988","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2025.151319_bib28","doi-asserted-by":"crossref","first-page":"7939","DOI":"10.1039\/C7DT01638G","article-title":"Reactions of persulfides with the heme cofactor of oxidized myoglobin and microperoxidase 11: reduction or coordination","volume":"46","author":"Galardon","year":"2017","journal-title":"Dalton Trans."},{"key":"10.1016\/j.bbrc.2025.151319_bib29","article-title":"Speciation of reactive sulfur species and their reactions with alkylating agents: do we have any clue about what is present inside the cell?: speciation of reactive sulfur species","author":"Bogd\u00e1ndi","year":"2018","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.bbrc.2025.151319_bib30","doi-asserted-by":"crossref","first-page":"513","DOI":"10.3891\/acta.chem.scand.53-0513","article-title":"Nucleophilic substitution of alkyl halides by electrogenerated polysulfide ions in N,N-dimethylacetamide","volume":"53","author":"Ahrika","year":"1999","journal-title":"Acta Chem. Scand."},{"key":"10.1016\/j.bbrc.2025.151319_bib31","doi-asserted-by":"crossref","first-page":"17172","DOI":"10.1002\/chem.201503353","article-title":"Solving the 170-year-old mystery about red-violet and blue transient intermediates in the gmelin reaction","volume":"21","author":"Gao","year":"2015","journal-title":"Chem. Eur J."},{"key":"10.1016\/j.bbrc.2025.151319_bib32","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1021\/ic50112a009","article-title":"Optical spectra and equilibrium distribution of polysulfide ions in aqueous solution at 20.deg","volume":"11","author":"Giggenbach","year":"1972","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib33","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/S0162-0134(99)00100-2","article-title":"Hemepeptide models for hemoproteins: the behavior of -acetylmicroperoxidase-11 in aqueous solution","volume":"75","author":"Marques","year":"1999","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbrc.2025.151319_bib34","doi-asserted-by":"crossref","first-page":"12275","DOI":"10.1021\/bi961042w","article-title":"Solution structure of horse heart ferricytochrome c and detection of redox-related structural changes by high-resolution1 H NMR","volume":"35","author":"Qi","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2025.151319_bib35","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1002\/jcc.20290","article-title":"The Amber biomolecular simulation programs","volume":"26","author":"Case","year":"2005","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib36","doi-asserted-by":"crossref","first-page":"1950","DOI":"10.1002\/prot.22711","article-title":"Improved side-chain torsion potentials for the Amber ff99SB protein force field","author":"Lindorff-Larsen","year":"2010","journal-title":"Proteins: Struct., Funct., Bioinf."},{"key":"10.1016\/j.bbrc.2025.151319_bib37","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0021-9991(77)90098-5","article-title":"Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes","volume":"23","author":"Ryckaert","year":"1977","journal-title":"J. Comput. Phys."},{"key":"10.1016\/j.bbrc.2025.151319_bib38","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1103\/PhysRevB.17.1302","article-title":"Molecular-dynamics study of a three-dimensional one-component model for distortive phase transitions","volume":"17","author":"Schneider","year":"1978","journal-title":"Phys. Rev. B"},{"key":"10.1016\/j.bbrc.2025.151319_bib39","doi-asserted-by":"crossref","first-page":"3684","DOI":"10.1063\/1.448118","article-title":"Molecular dynamics with coupling to an external bath","volume":"81","author":"Berendsen","year":"1984","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbrc.2025.151319_bib40","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1002\/jcc.25754","article-title":"On the accurate estimation of free energies using the jarzynski equality","volume":"40","author":"Arrar","year":"2019","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib41","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.1103\/PhysRevLett.78.2690","article-title":"Nonequilibrium equality for free energy differences","volume":"78","author":"Jarzynski","year":"1997","journal-title":"Phys. Rev. Lett."},{"key":"10.1016\/j.bbrc.2025.151319_bib42","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1021\/ct400308n","article-title":"GPU accelerated implementation of density functional theory for hybrid QM\/MM simulations","volume":"10","author":"Nitsche","year":"2014","journal-title":"J. Chem. Theor. Comput."},{"key":"10.1016\/j.bbrc.2025.151319_bib43","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2018.00070","article-title":"Chemical reactivity and spectroscopy explored from QM\/MM molecular dynamics simulations using the LIO code","volume":"6","author":"Marcolongo","year":"2018","journal-title":"Front. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib44","doi-asserted-by":"crossref","first-page":"13728","DOI":"10.1021\/jp036236h","article-title":"A DFT-based QM-MM approach designed for the treatment of large molecular systems: application to chorismate mutase","volume":"107","author":"Crespo","year":"2003","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbrc.2025.151319_bib45","doi-asserted-by":"crossref","first-page":"5029","DOI":"10.1063\/1.478401","article-title":"Assessment of the perdew\u2013burke\u2013ernzerhof exchange-correlation functional","volume":"110","author":"Ernzerhof","year":"1999","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbrc.2025.151319_bib46","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1139\/v92-079","article-title":"Optimization of Gaussian-type basis sets for local spin density functional calculations. Part I. Boron through neon, optimization technique and validation","volume":"70","author":"Godbout","year":"1992","journal-title":"Can. J. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib47","doi-asserted-by":"crossref","first-page":"3696","DOI":"10.1021\/acs.jctc.5b00255","article-title":"ff14SB: improving the accuracy of protein side chain and backbone parameters from ff99SB","volume":"11","author":"Maier","year":"2015","journal-title":"J. Chem. Theor. Comput."},{"key":"10.1016\/j.bbrc.2025.151319_bib48","doi-asserted-by":"crossref","first-page":"2609","DOI":"10.1021\/acs.jcim.2c01522","article-title":"Best practices on QM\/MM simulations of biological systems","volume":"63","author":"Clemente","year":"2023","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.bbrc.2025.151319_bib49","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2021.111455","article-title":"Distal lysine (de)coordination in the algal hemoglobin THB1: A combined computer simulation and experimental study","volume":"220","author":"Juli\u00f3 Plana","year":"2021","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbrc.2025.151319_bib50","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-11259-0","article-title":"Tertiary and quaternary structural basis of oxygen affinity in human hemoglobin as revealed by multiscale simulations","volume":"7","author":"Bringas","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbrc.2025.151319_bib51","doi-asserted-by":"crossref","first-page":"12817","DOI":"10.1021\/ja062876x","article-title":"The catalytic mechanism of peptidylglycine \u03b1-hydroxylating monooxygenase investigated by computer simulation","volume":"128","author":"Crespo","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbrc.2025.151319_bib52","series-title":"Classical and Quantum Dynamics in Condensed Phase Simulations","first-page":"385","article-title":"Nudged elastic band method for finding minimum energy paths of transitions","author":"J\u00f3nsson","year":"1998"},{"key":"10.1016\/j.bbrc.2025.151319_bib53","doi-asserted-by":"crossref","first-page":"9978","DOI":"10.1063\/1.1323224","article-title":"Improved tangent estimate in the nudged elastic band method for finding minimum energy paths and saddle points","volume":"113","author":"Henkelman","year":"2000","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbrc.2025.151319_bib54","series-title":"Theoretical Methods in Condensed Phase Chemistry","year":"2002"},{"key":"10.1016\/j.bbrc.2025.151319_bib55","doi-asserted-by":"crossref","first-page":"3631","DOI":"10.1021\/acs.inorgchem.9b03198","article-title":"In silico insight into the reductive nitrosylation of ferric hemeproteins","volume":"59","author":"Foglia","year":"2020","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib56","doi-asserted-by":"crossref","first-page":"9907","DOI":"10.1021\/acs.inorgchem.4c00833","article-title":"Mechanism of peroxynitrite interaction with ferric M. tuberculosis nitrobindin: a computational study","volume":"63","author":"Messias","year":"2024","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib57","doi-asserted-by":"crossref","DOI":"10.1103\/PhysRevLett.97.170201","article-title":"Structural relaxation made simple","volume":"97","author":"Bitzek","year":"2006","journal-title":"Phys. Rev. Lett."},{"key":"10.1016\/j.bbrc.2025.151319_bib58","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1007\/s00775-016-1361-z","article-title":"Cyanide binding to ferrous and ferric microperoxidase-11","volume":"21","author":"Ascenzi","year":"2016","journal-title":"JBIC, J. Biol. Inorg. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib59","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. Biol. Chem."},{"key":"10.1016\/j.bbrc.2025.151319_bib60","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.jinorgbio.2018.02.007","article-title":"Reactions of ferric hemoglobin and myoglobin with hydrogen sulfide under physiological conditions","volume":"182","author":"Jensen","year":"2018","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbrc.2025.151319_bib61","doi-asserted-by":"crossref","first-page":"8476","DOI":"10.1021\/jacs.6b03456","article-title":"Hydrogen sulfide oxidation by myoglobin","volume":"138","author":"Bostelaar","year":"2016","journal-title":"J. Am. Chem. Soc."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X25000336?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X25000336?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T18:04:45Z","timestamp":1777399485000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X25000336"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2]]},"references-count":61,"alternative-id":["S0006291X25000336"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2025.151319","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2025,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Coordination of inorganic disulfide species to ferric N-acetyl microperoxidase 11","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrc.2025.151319","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"151319"}}