{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T11:42:05Z","timestamp":1791027725591,"version":"4.1.0"},"reference-count":31,"publisher":"National Academy of Sciences","issue":"15","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2000,7,18]]},"abstract":"<jats:p>\n                    In a recent article [Khan, A. U., Kovacic, D., Kolbanovsky, A., Desai, M., Frenkel, K. &amp; Geacintov, N. E. (2000)\n                    <jats:italic>Proc. Natl. Acad. Sci. USA<\/jats:italic>\n                    97, 2984\u20132989], the authors claimed that ONOO\n                    <jats:sup>\u2212<\/jats:sup>\n                    , after protonation to ONOOH, decomposes into\n                    <jats:sup>1<\/jats:sup>\n                    HNO and\n                    <jats:sup>1<\/jats:sup>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    according to a spin-conserved unimolecular mechanism. This claim was based partially on their observation that nitrosylhemoglobin is formed via the reaction of peroxynitrite with methemoglobin at neutral pH. However, thermochemical considerations show that the yields of\n                    <jats:sup>1<\/jats:sup>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    and\n                    <jats:sup>1<\/jats:sup>\n                    HNO are about 23 orders of magnitude lower than those of\n                    <jats:sup>\u22c5<\/jats:sup>\n                    NO\n                    <jats:sub>2<\/jats:sub>\n                    and\n                    <jats:sup>\u22c5<\/jats:sup>\n                    OH, which are formed via the homolysis of ONOOH. We also show that methemoglobin does not form with peroxynitrite any spectrally detectable product, but with contaminations of nitrite and H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    present in the peroxynitrite sample. Thus, there is no need to modify the present view of the mechanism of ONOOH decomposition, according to which initial homolysis into a radical pair, [ONO\n                    <jats:sup>\u22c5<\/jats:sup>\n                    <jats:sup>\u22c5<\/jats:sup>\n                    OH]\n                    <jats:sub>cage<\/jats:sub>\n                    , is followed by the diffusion of about 30% of the radicals out of the cage, while the rest recombines to nitric acid in the solvent cage.\n                  <\/jats:p>","DOI":"10.1073\/pnas.150238197","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:41:48Z","timestamp":1027680108000},"page":"8216-8218","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":26,"title":["The decomposition of peroxynitrite does not yield nitroxyl anion and singlet oxygen"],"prefix":"10.1073","volume":"97","author":[{"given":"G\u00e1bor","family":"Mer\u00e9nyi","sequence":"first","affiliation":[{"name":"Department of Chemistry, Nuclear Chemistry, The Royal Institute of Technology, S-10044 Stockholm 70, Sweden; and Department of Physical Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Johan","family":"Lind","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Nuclear Chemistry, The Royal Institute of Technology, S-10044 Stockholm 70, Sweden; and Department of Physical Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gidon","family":"Czapski","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Nuclear Chemistry, The Royal Institute of Technology, S-10044 Stockholm 70, Sweden; and Department of Physical Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara","family":"Goldstein","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Nuclear Chemistry, The Royal Institute of Technology, S-10044 Stockholm 70, Sweden; and Department of Physical Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2000,7,4]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00717a019"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1021\/tx00030a017"},{"key":"e_1_3_3_3_2","first-page":"L699","volume":"288","author":"Pryor W A","year":"1995","unstructured":"W A Pryor, G L Squadrito Am J Physiol 288, L699\u2013L722 (1995).","journal-title":"Am J Physiol"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0891-5849(96)00280-8"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1021\/tx970101j"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1021\/tx970200x"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1021\/tx980500u"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1021\/tx980026s"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1021\/jp984686h"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja991077u"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1021\/ic990384y"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.6.3465"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja982887t"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.97.7.2984"},{"key":"e_1_3_3_15_2","first-page":"472","volume-title":"Oxygenases","author":"Wang J H","year":"1962","unstructured":"J H Wang Oxygenases, ed O Hayaishi (Academic, New York), pp. 472 (1962)."},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0891-5849(97)00365-1"},{"key":"e_1_3_3_17_2","first-page":"280","volume-title":"Hemoglobin and Myoglobin in Their Reactions with Ligands","author":"Antonini E","year":"1971","unstructured":"E Antonini, M Brunori Hemoglobin and Myoglobin in Their Reactions with Ligands (North\u2014Holland, Amsterdam), pp. 280 (1971)."},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(91)90452-O"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00020a014"},{"key":"e_1_3_3_20_2","volume-title":"J. 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