{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T15:48:54Z","timestamp":1787240934748,"version":"build-2736575974"},"reference-count":66,"publisher":"SAGE Publications","issue":"4","license":[{"start":{"date-parts":[[2020,1,2]],"date-time":"2020-01-02T00:00:00Z","timestamp":1577923200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["Antioxidants &amp; Redox Signaling"],"published-print":{"date-parts":[[2020,2]]},"abstract":"<jats:sec>\n                    <jats:title>Significance:<\/jats:title>\n                    <jats:p>\n                      Sulfides are endogenous and ubiquitous signaling species that share the hemeproteins as biochemical targets with O\n                      <jats:sub>2<\/jats:sub>\n                      , nitric oxide, and carbon monoxide. The description of the binding mechanisms is mandatory to anticipate the biochemical relevance of the interaction.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Recent Advances:<\/jats:title>\n                    <jats:p>\n                      The binding of sulfide to ferric hemeproteins has been described in more than 40 systems, including native proteins, mutants, and model systems. Mechanisms of sulfide binding to ferric hemeproteins have been examined by a combination of kinetic and computational experiments. The distal control of the association process, dissected into the migration of the ligand to the active site and the binding event, reveals that neutral hydrogen sulfide (H\n                      <jats:sub>2<\/jats:sub>\n                      S) reaches the active site and is the predominant binding ligand, while the HS\n                      <jats:sup>\u2212<\/jats:sup>\n                      is excluded by the protein matrix. Experiments with model compounds, devoid of a protein scaffold, reveal that both H\n                      <jats:sub>2<\/jats:sub>\n                      S and HS\n                      <jats:sup>\u2212<\/jats:sup>\n                      can bind the ferric heme if accessing the site. A critical role of the proximal ligand in the prevention of the metal-centered reduction has been experimentally assessed. For metmyoglobin and methemoglobin, the coordination of sulfide leads to noncanonical functions: sulfide storage and its oxidative detoxification have been evidenced under physiological and excess sulfide concentrations, respectively.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Critical Issues:<\/jats:title>\n                    <jats:p>The bound species is suggested to predominate in the monoprotonated form, although spectroscopic evidence is pending.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Future Directions:<\/jats:title>\n                    <jats:p>A description of the role of hemeproteins as biochemical targets for inorganic sulfide requires understanding the reactivity of bound sulfide, for example: the metal-centered reduction, the reaction with excess sulfide, oxidants, or other gasotransmitters, among other biomolecules.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1089\/ars.2019.7878","type":"journal-article","created":{"date-parts":[[2019,9,18]],"date-time":"2019-09-18T07:30:36Z","timestamp":1568791836000},"page":"247-257","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":33,"title":["Hemeproteins as Targets for Sulfide Species"],"prefix":"10.1177","volume":"32","author":[{"given":"Fernando Mart\u00edn","family":"Boubeta","sequence":"first","affiliation":[{"name":"Instituto de Qu\u00edmica F\u00edsica de los Materiales, Medio Ambiente y Energ\u00eda. (INQUIMAE) CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvina Andrea","family":"Bieza","sequence":"additional","affiliation":[{"name":"Instituto de Qu\u00edmica F\u00edsica de los Materiales, Medio Ambiente y Energ\u00eda. (INQUIMAE) CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mauro","family":"Bringas","sequence":"additional","affiliation":[{"name":"Instituto de Qu\u00edmica F\u00edsica de los Materiales, Medio Ambiente y Energ\u00eda. (INQUIMAE) CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina."},{"name":"Departamento de Qu\u00edmica Inorg\u00e1nica, Anal\u00edtica y Qu\u00edmica F\u00edsica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juan Cruz","family":"Palermo","sequence":"additional","affiliation":[{"name":"Instituto de Qu\u00edmica F\u00edsica de los Materiales, Medio Ambiente y Energ\u00eda. (INQUIMAE) CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leonardo","family":"Boechi","sequence":"additional","affiliation":[{"name":"Facultad de Ciencias Exactas y Naturales, Instituto de C\u00e1lculo, Universidad de Buenos Aires, Buenos Aires, Argentina."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dar\u00edo Ariel","family":"Estrin","sequence":"additional","affiliation":[{"name":"Instituto de Qu\u00edmica F\u00edsica de los Materiales, Medio Ambiente y Energ\u00eda. (INQUIMAE) CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina."},{"name":"Departamento de Qu\u00edmica Inorg\u00e1nica, Anal\u00edtica y Qu\u00edmica F\u00edsica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara Elizabeth","family":"Bari","sequence":"additional","affiliation":[{"name":"Instituto de Qu\u00edmica F\u00edsica de los Materiales, Medio Ambiente y Energ\u00eda. 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