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Lett."},{"key":"10.1016\/j.jinorgbio.2021.111633_bb0580","doi-asserted-by":"crossref","first-page":"6947","DOI":"10.1021\/jo8012836","article-title":"Regiospecifically \u03b1-13C-labeled porphyrins for studies of ground-state hole transfer in multiporphyrin arrays","volume":"73","author":"Muresan","year":"2008","journal-title":"J. Org. Chem."},{"key":"10.1016\/j.jinorgbio.2021.111633_bb0585","doi-asserted-by":"crossref","first-page":"5754","DOI":"10.1021\/ic0105866","article-title":"(F8TPP)FeII\/O2 Reactivity Studies {F8TPP = Tetrakis(2,6-difluorophenyl)porphyrinate(2\u2212)}: Spectroscopic (UV\u2212Visible and NMR) and Kinetic Study of Solvent-Dependent (Fe\/O2 = 1:1 or 2:1) Reversible O2-Reduction and Ferryl Formation","volume":"40","author":"Ghiladi","year":"2001","journal-title":"Inorg. 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Lett."},{"key":"10.1016\/j.jinorgbio.2021.111633_bb0705","doi-asserted-by":"crossref","first-page":"2614","DOI":"10.1021\/ic802123m","article-title":"Effect of imidazole and Phenolate axial ligands on the electronic structure and reactivity of Oxoiron(IV) porphyrin \u03c0-cation radical complexes: drastic increase in oxo-transfer and hydrogen abstraction reactivities","volume":"48","author":"Takahashi","year":"2009","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2021.111633_bb0710","doi-asserted-by":"crossref","first-page":"5572","DOI":"10.1021\/ic000502d","article-title":"Effect of anionic axial ligands on the formation of oxoiron(IV) porphyrin intermediates","volume":"39","author":"Nam","year":"2000","journal-title":"Inorg. 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Soc."},{"key":"10.1016\/j.jinorgbio.2021.111633_bb0735","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1038\/nchembio.2007.46","article-title":"Catalytic generation of N2O3 by the concerted nitrite reductase and anhydrase activity of hemoglobin","volume":"3","author":"Basu","year":"2007","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jinorgbio.2021.111633_bb0740","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1007\/BF03401781","article-title":"Inducible nitric oxide synthase and inflammatory diseases","volume":"6","author":"Zamora","year":"2000","journal-title":"Mol. Med."},{"key":"10.1016\/j.jinorgbio.2021.111633_bb0745","doi-asserted-by":"crossref","first-page":"763","DOI":"10.2741\/1268","article-title":"Nitric oxide neurotoxicity in neurodegenerative diseases","volume":"9","author":"Boje","year":"2004","journal-title":"Front. 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Those additional pathways possibly include: (1) the direct oxidation of NO by mCPBA giving NO2 (although in low yields), and (2) a second reactivity cycle resulting from the re-oxidation of final Fe(III) complex by leftover mCPBA to regenerate Cmpd-I, which could then go on to react with excess NO in solution producing NO2."},{"key":"10.1016\/j.jinorgbio.2021.111633_bb0800","unstructured":"No evidence of [(Por)Cmpd-II] was observed during these reactions even at cryogenic conditions, ruling out the initial conversion of NO to NO2\u2212 upon its reactivity with [(Por)Cmpd-I]."}],"container-title":["Journal of Inorganic Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013421002804?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013421002804?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,27]],"date-time":"2025-09-27T15:05:53Z","timestamp":1758985553000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0162013421002804"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,1]]},"references-count":160,"alternative-id":["S0162013421002804"],"URL":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2021.111633","relation":{},"ISSN":["0162-0134"],"issn-type":[{"value":"0162-0134","type":"print"}],"subject":[],"published":{"date-parts":[[2022,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Bio-inspired nitrogen oxide (NOx) interconversion reactivities of synthetic heme Compound-I and Compound-II intermediates","name":"articletitle","label":"Article Title"},{"value":"Journal of Inorganic Biochemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2021.111633","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier Inc. 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