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Cell Res."},{"key":"10.1016\/j.redox.2023.102617_bib60","series-title":"Biological Inorganic Chemistry","first-page":"69","article-title":"Chapter 4 - biological ligands for metal ions","author":"Crichton","year":"2012"},{"issue":"2","key":"10.1016\/j.redox.2023.102617_bib61","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1007\/s00775-007-0318-7","article-title":"Iron-sulfur protein folds, iron-sulfur chemistry, and evolution","volume":"13","author":"Meyer","year":"2008","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/j.redox.2023.102617_bib62","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1146\/annurev.biochem.74.082803.133518","article-title":"Structure, function, and formation of biological iron-sulfur clusters","volume":"74","author":"Johnson","year":"2005","journal-title":"Annu. Rev. Biochem."},{"issue":"31","key":"10.1016\/j.redox.2023.102617_bib63","doi-asserted-by":"crossref","first-page":"12754","DOI":"10.1074\/jbc.R117.787101","article-title":"Iron-sulfur cluster biogenesis and trafficking in mitochondria","volume":"292","author":"Braymer","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2023.102617_bib64","series-title":"Microbial Iron Metabolism","first-page":"161","article-title":"Chapter 8 \u2013 ferredoxin and rubredoxin","author":"Lovenberg","year":"1974"},{"key":"10.1016\/j.redox.2023.102617_bib65","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2021.102164","article-title":"Mitochondrial iron-sulfur clusters: structure, function, and an emerging role in vascular biology","volume":"47","author":"Read","year":"2021","journal-title":"Redox Biol."},{"issue":"11","key":"10.1016\/j.redox.2023.102617_bib66","doi-asserted-by":"crossref","DOI":"10.3390\/antiox10111738","article-title":"Sulfur administration in Fe\u2013S cluster homeostasis","volume":"10","author":"Rydz","year":"2021","journal-title":"Antioxidants"},{"issue":"8","key":"10.1016\/j.redox.2023.102617_bib67","doi-asserted-by":"crossref","first-page":"a011312","DOI":"10.1101\/cshperspect.a011312","article-title":"The role of mitochondria in cellular iron-sulfur protein biogenesis: mechanisms, connected processes, and diseases","volume":"5","author":"Stehling","year":"2013","journal-title":"Cold Spring Harbor Perspect. Biol."},{"issue":"1","key":"10.1016\/j.redox.2023.102617_bib68","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1080\/10409230701829169","article-title":"The radical SAM superfamily","volume":"43","author":"Frey","year":"2008","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"issue":"33","key":"10.1016\/j.redox.2023.102617_bib69","doi-asserted-by":"crossref","first-page":"11589","DOI":"10.1073\/pnas.0805713105","article-title":"A newly discovered role for iron-sulfur clusters","volume":"105","author":"Dos Santos","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"11\u201312","key":"10.1016\/j.redox.2023.102617_bib70","doi-asserted-by":"crossref","first-page":"2276","DOI":"10.1016\/j.freeradbiomed.2012.04.007","article-title":"Analytical measurement of discrete hydrogen sulfide pools in biological specimens","volume":"52","author":"Shen","year":"2012","journal-title":"Free Radic. Biol. Med."},{"issue":"2","key":"10.1016\/j.redox.2023.102617_bib71","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1089\/ars.2010.3525","article-title":"Free and acid-labile hydrogen sulfide concentrations in mouse tissues: anomalously high free hydrogen sulfide in aortic tissue","volume":"15","author":"Levitt","year":"2011","journal-title":"Antioxidants Redox Signal."},{"issue":"2","key":"10.1016\/j.redox.2023.102617_bib72","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1089\/ars.2008.2132","article-title":"A source of hydrogen sulfide and a mechanism of its release in the brain","volume":"11","author":"Ishigami","year":"2009","journal-title":"Antioxidants Redox Signal."},{"issue":"1","key":"10.1016\/j.redox.2023.102617_bib73","doi-asserted-by":"crossref","first-page":"3566","DOI":"10.1038\/s41467-019-11470-9","article-title":"Physiologically relevant reconstitution of iron-sulfur cluster biosynthesis uncovers persulfide-processing functions of ferredoxin-2 and frataxin","volume":"10","author":"Gervason","year":"2019","journal-title":"Nat. Commun."},{"issue":"7","key":"10.1016\/j.redox.2023.102617_bib74","doi-asserted-by":"crossref","first-page":"2754","DOI":"10.1073\/pnas.90.7.2754","article-title":"Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis","volume":"90","author":"Zheng","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"7\u20138","key":"10.1016\/j.redox.2023.102617_bib75","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.ccr.2010.10.016","article-title":"Structural, Mechanistic and coordination chemistry of relevance to the biosynthesis of iron-sulfur and related iron cofactors","volume":"255","author":"Qi","year":"2011","journal-title":"Coord. Chem. Rev."},{"key":"10.1016\/j.redox.2023.102617_bib76","doi-asserted-by":"crossref","first-page":"5686","DOI":"10.1038\/ncomms6686","article-title":"Mammalian frataxin directly enhances sulfur transfer of NFS1 persulfide to both ISCU and free thiols","volume":"6","author":"Parent","year":"2015","journal-title":"Nat. Commun."},{"issue":"2","key":"10.1016\/j.redox.2023.102617_bib77","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1242\/dmm.009019","article-title":"Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease","volume":"5","author":"Rouault","year":"2012","journal-title":"Dis. Model. Mech."},{"issue":"1","key":"10.1016\/j.redox.2023.102617_bib78","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/s40673-021-00140-6","article-title":"Rare occurrence of severe blindness and deafness in Friedreich ataxia: a case report","volume":"8","author":"Damasio","year":"2021","journal-title":"Cerebellum Ataxias"},{"issue":"5","key":"10.1016\/j.redox.2023.102617_bib79","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1016\/j.febslet.2008.01.046","article-title":"Overexpression of frataxin in the mitochondria increases resistance to oxidative stress and extends lifespan in Drosophila","volume":"582","author":"Runko","year":"2008","journal-title":"FEBS Lett."},{"issue":"1","key":"10.1016\/j.redox.2023.102617_bib80","doi-asserted-by":"crossref","first-page":"eaax8358","DOI":"10.1126\/sciadv.aax8358","article-title":"Control of protein function through oxidation and reduction of persulfidated states","volume":"6","author":"Doka","year":"2020","journal-title":"Sci. Adv."},{"issue":"45","key":"10.1016\/j.redox.2023.102617_bib81","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2100050118","article-title":"Reprogrammed transsulfuration promotes basal-like breast tumor progression via realigning cellular cysteine persulfidation","volume":"118","author":"Erdelyi","year":"2021","journal-title":"Proc. Natl. Acad. Sci. 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Sci."},{"issue":"4","key":"10.1016\/j.redox.2023.102617_bib86","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1089\/ars.2019.7878","article-title":"Hemeproteins as targets for sulfide species","volume":"32","author":"Boubeta","year":"2020","journal-title":"Antioxidants Redox Signal."},{"issue":"18","key":"10.1016\/j.redox.2023.102617_bib87","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1089\/ars.2020.8171","article-title":"Red blood cells as a \"central hub\" for sulfide bioactivity: scavenging, metabolism, transport, and cross-talk with nitric oxide","volume":"33","author":"Cortese-Krott","year":"2020","journal-title":"Antioxidants Redox Signal."},{"issue":"1","key":"10.1016\/j.redox.2023.102617_bib88","doi-asserted-by":"crossref","DOI":"10.3390\/ijms22010047","article-title":"Therapeutic potential of carbon monoxide (CO) and hydrogen sulfide (H2S) in hemolytic and hemorrhagic vascular disorders-interaction between the heme oxygenase and H2S-producing systems","volume":"22","author":"Gall","year":"2020","journal-title":"Int. J. Mol. Sci."},{"issue":"12","key":"10.1016\/j.redox.2023.102617_bib89","doi-asserted-by":"crossref","first-page":"13098","DOI":"10.1096\/fj.201901304R","article-title":"Hydrogen sulfide signaling in mitochondria and disease","volume":"33","author":"Murphy","year":"2019","journal-title":"Faseb. J."},{"issue":"2","key":"10.1016\/j.redox.2023.102617_bib90","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1089\/ars.2010.3698","article-title":"Hydrogen sulfide and hemeproteins: knowledge and mysteries","volume":"15","author":"Pietri","year":"2011","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.redox.2023.102617_bib91","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.jinorgbio.2014.01.013","article-title":"Hydrogen sulfide activation in hemeproteins: the sulfheme scenario","volume":"133","author":"Rios-Gonzalez","year":"2014","journal-title":"J. Inorg. 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Res."},{"issue":"4","key":"10.1016\/j.redox.2023.102617_bib95","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1089\/ars.2019.7877","article-title":"A novel possible role for met hemoglobin as carrier of hydrogen sulfide in the blood","volume":"32","author":"Jensen","year":"2020","journal-title":"Antioxidants Redox Signal."},{"issue":"22","key":"10.1016\/j.redox.2023.102617_bib96","doi-asserted-by":"crossref","first-page":"4881","DOI":"10.1021\/bi801738j","article-title":"Factors controlling the reactivity of hydrogen sulfide with hemeproteins","volume":"48","author":"Pietri","year":"2009","journal-title":"Biochemistry"},{"issue":"1","key":"10.1016\/j.redox.2023.102617_bib97","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0021-9258(18)73923-9","article-title":"A study of sulfhemoglobin","volume":"126","author":"Michel","year":"1938","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.redox.2023.102617_bib98","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1016\/j.bbrc.2010.08.068","article-title":"Structural determinants for the formation of sulfhemeprotein complexes","volume":"400","author":"Roman-Morales","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"23","key":"10.1016\/j.redox.2023.102617_bib99","doi-asserted-by":"crossref","first-page":"7366","DOI":"10.1016\/S0021-9258(19)45895-X","article-title":"Sulfheme proteins. II. The reversible oxygenation of ferrous sulfmyoglobin","volume":"246","author":"Berzofsky","year":"1971","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.redox.2023.102617_bib100","doi-asserted-by":"crossref","first-page":"2883","DOI":"10.1021\/jf305363e","article-title":"Reduction of ferrylmyoglobin by hydrogen sulfide. Kinetics in relation to meat greening","volume":"61","author":"Libardi","year":"2013","journal-title":"J. Agric. Food Chem."},{"issue":"2","key":"10.1016\/j.redox.2023.102617_bib101","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1042\/bj0810374","article-title":"The formation and properties of sulphmyoglobin and sulphcatalase","volume":"81","author":"Nicholls","year":"1961","journal-title":"Biochem. J."},{"issue":"11","key":"10.1016\/j.redox.2023.102617_bib102","doi-asserted-by":"crossref","first-page":"7080","DOI":"10.1016\/S0021-9258(17)39840-X","article-title":"Reactions of ferryl lactoperoxidase (compound II) with sulfide and sulfhydryl compounds","volume":"259","author":"Nakamura","year":"1984","journal-title":"J. Biol. 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Chem."},{"key":"10.1016\/j.redox.2023.102617_bib109","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1289\/ehp.8564321","article-title":"Free-radical production and oxidative reactions of hemoglobin","volume":"64","author":"Winterbourn","year":"1985","journal-title":"Environ. Health Perspect."},{"issue":"2","key":"10.1016\/j.redox.2023.102617_bib110","doi-asserted-by":"crossref","first-page":"134","DOI":"10.3109\/07388551.2012.732031","article-title":"Human cytochrome b5 reductase: structure, function, and potential applications","volume":"34","author":"Elahian","year":"2014","journal-title":"Crit. Rev. Biotechnol."},{"key":"10.1016\/j.redox.2023.102617_bib111","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.bcp.2018.01.045","article-title":"Investigations on the role of hemoglobin in sulfide metabolism by intact human red blood cells","volume":"149","author":"Bianco","year":"2018","journal-title":"Biochem. Pharmacol."},{"issue":"2","key":"10.1016\/j.redox.2023.102617_bib112","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1373\/clinchem.2004.035154","article-title":"Laboratory assessment of oxygenation in methemoglobinemia","volume":"51","author":"Haymond","year":"2005","journal-title":"Clin. Chem."},{"issue":"2","key":"10.1016\/j.redox.2023.102617_bib113","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1002\/ajh.20738","article-title":"Methemoglobin\u2014it's not just blue: a concise review","volume":"82","author":"Umbreit","year":"2007","journal-title":"Am. J. Hematol."},{"issue":"784","key":"10.1016\/j.redox.2023.102617_bib114","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1098\/rspb.1933.0056","article-title":"On the combinations of meth\u00e6moglobin with H2S","volume":"113","author":"Keilin","year":"1933","journal-title":"Proc. Roy. Soc. Lond. B."},{"issue":"27","key":"10.1016\/j.redox.2023.102617_bib115","doi-asserted-by":"crossref","first-page":"16043","DOI":"10.1016\/S0021-9258(17)46185-0","article-title":"Hemoglobins of the Lucina pectinata\/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands","volume":"265","author":"Kraus","year":"1990","journal-title":"J. Biol. Chem."},{"issue":"27","key":"10.1016\/j.redox.2023.102617_bib116","doi-asserted-by":"crossref","first-page":"16054","DOI":"10.1016\/S0021-9258(17)46186-2","article-title":"Hemoglobins of the Lucina pectinata\/bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins","volume":"265","author":"Kraus","year":"1990","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.redox.2023.102617_bib117","first-page":"60","article-title":"The role of hydrogen sulfide in evolution and the evolution of hydrogen sulfide in metabolism and signaling","volume":"31","author":"Olson","year":"2016","journal-title":"Physiology (Bethesda, Md"},{"issue":"36","key":"10.1016\/j.redox.2023.102617_bib118","doi-asserted-by":"crossref","first-page":"9642","DOI":"10.1021\/acs.jpcb.6b06686","article-title":"Access and binding of H2S to hemeproteins: the case of HbI of Lucina pectinata","volume":"120","author":"Boubeta","year":"2016","journal-title":"J. Phys. Chem. B"},{"issue":"4","key":"10.1016\/j.redox.2023.102617_bib119","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1023\/B:JOPC.0000027848.40972.97","article-title":"Functional characterization of the purified holo form of hemoglobin I from Lucina pectinata overexpressed in Escherichia coli","volume":"23","author":"Collazo","year":"2004","journal-title":"Prot. J."},{"issue":"2","key":"10.1016\/j.redox.2023.102617_bib120","first-page":"184","article-title":"High-level production of recombinant sulfide-reactive hemoglobin I from Lucina pectinata in Escherichia coli. High yields of fully functional holoprotein synthesis in the BLi5 E. coli strain","volume":"38","author":"Le\u00f3n","year":"2004","journal-title":"Protein Expr. Purif."},{"issue":"7","key":"10.1016\/j.redox.2023.102617_bib121","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1080\/08927020802144114","article-title":"Effects of active site mutations in haemoglobin I from Lucina pectinata: a molecular dynamic study","volume":"34","author":"Ramirez","year":"2008","journal-title":"Mol. Simulat."},{"key":"10.1016\/j.redox.2023.102617_bib122","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."},{"issue":"1","key":"10.1016\/j.redox.2023.102617_bib123","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/0041-008X(66)90112-8","article-title":"On the mechanism of sulfide inactivation by methemoglobin","volume":"8","author":"Smith","year":"1966","journal-title":"Toxicol. Appl. Pharmacol."},{"issue":"13","key":"10.1016\/j.redox.2023.102617_bib124","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."},{"issue":"7","key":"10.1016\/j.redox.2023.102617_bib125","doi-asserted-by":"crossref","first-page":"3916","DOI":"10.1021\/acs.inorgchem.6b02878","article-title":"Mechanism of reduction of ferric porphyrins by sulfide: identification of a low spin Fe(III)-SH intermediate","volume":"56","author":"Mittra","year":"2017","journal-title":"Inorg. Chem."},{"issue":"27","key":"10.1016\/j.redox.2023.102617_bib126","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. 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