{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T17:16:46Z","timestamp":1788369406570,"version":"build-2803163510"},"reference-count":54,"publisher":"American Chemical Society (ACS)","issue":"10","license":[{"start":{"date-parts":[[2015,9,19]],"date-time":"2015-09-19T00:00:00Z","timestamp":1442620800000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_ccby_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100005851","name":"John Simon Guggenheim Memorial Foundation","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/100005851","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":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100002923","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003074","name":"Agencia Nacional de Promoci\u00f3n Cient\u00edfica y Tecnol\u00f3gica","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100003074","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,10,21]]},"abstract":"<jats:title>Conspectus<\/jats:title>\n                  <jats:p>Azanone (1HNO, nitroxyl) shows interesting yet poorly understood chemical and biological effects. HNO has some overlapping properties with nitric oxide (NO), sharing its biological reactivity toward heme proteins, thiols, and oxygen. Despite this similarity, HNO and NO show significantly different pharmacological effects. The high reactivity of HNO means that studies must rely on the use of donor molecules such as trioxodinitrate (Angeli\u2019s salt). It has been suggested that azanone could be an intermediate in several reactions and that it may be an enzymatically produced signaling molecule. The inherent difficulty in detecting its presence unequivocally prevents evidence from yielding definite answers. On the other hand, metalloporphyrins are widely used as chemical models of heme proteins, providing us with invaluable tools for the study of the coordination chemistry of small molecules, like NO, CO, and O2. Studies with transition metal porphyrins have shown diverse mechanistic, kinetic, structural, and reactive aspects related to the formation of nitrosyl complexes. Porphyrins are also widely used in technical applications, especially when coupled to a surface, where they can be used as electrochemical gas sensors. Given their versatility, they have not escaped their role as key players in chemical studies involving HNO.<\/jats:p>\n                  <jats:p>This Account presents the research performed during the last 10 years in our group concerning azanone reactions with iron, manganese, and cobalt porphyrins. We begin by describing their HNO trapping capabilities, which result in formation of the corresponding nitrosyl complexes. Kinetic and mechanistic studies of these reactions show two alternative operating mechanisms: reaction of the metal center with HNO or with the donor. Moreover, we have also shown that azanone can be stabilized by coordination to iron porphyrins using electron-attracting substituents attached to the porphyrin ring, which balance the negatively charged NO\u00af.<\/jats:p>\n                  <jats:p>Second, we describe an electrochemical HNO sensing device based on the covalent attachment of a cobalt porphyrin to gold. A surface effect affects the redox potentials and allows discrimination between HNO and NO. The reaction with the former is fast, efficient, and selective, lacking spurious signals due to the presence of reactive nitrogen and oxygen species. The sensor is both biologically compatible and highly sensitive (nanomolar). This time-resolved detection allows kinetic analysis of reactions producing HNO. The sensor thus offers excellent opportunities to be used in experiments looking for HNO. As examples, we present studies concerning (a) HNO donation capabilities of new HNO donors as assessed by the sensor, (b) HNO detection as an intermediate in O atom abstraction to nitrite by phosphines, and (c) NO to HNO interconversion mediated by alcohols and thiols.<\/jats:p>\n                  <jats:p>Finally, we briefly discuss the key experiments required to demonstrate endogenous HNO formation to be done in the near future, involving the in vivo use of the HNO sensing device.<\/jats:p>","DOI":"10.1021\/ar500153c","type":"journal-article","created":{"date-parts":[[2014,9,19]],"date-time":"2014-09-19T15:15:19Z","timestamp":1411139719000},"page":"2907-2916","source":"Crossref","is-referenced-by-count":67,"title":["Reactions of HNO with Metal Porphyrins: Underscoring\nthe Biological Relevance of HNO"],"prefix":"10.1021","volume":"47","author":[{"given":"Fabio","family":"Doctorovich","sequence":"first","affiliation":[{"name":"Universidad de Buenos Aires, Ciudad Universitaria , , Pab. II (1428) , ,","place":["Buenos Aires, Argentina"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Damian E.","family":"Bikiel","sequence":"additional","affiliation":[{"name":"Universidad de Buenos Aires, Ciudad Universitaria , , Pab. II (1428) , ,","place":["Buenos Aires, Argentina"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juan","family":"Pellegrino","sequence":"additional","affiliation":[{"name":"Universidad de Buenos Aires, Ciudad Universitaria , , Pab. II (1428) , ,","place":["Buenos Aires, Argentina"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sebastia\u0301n A.","family":"Sua\u0301rez","sequence":"additional","affiliation":[{"name":"Universidad de Buenos Aires, Ciudad Universitaria , , Pab. II (1428) , ,","place":["Buenos Aires, Argentina"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcelo A.","family":"Marti\u0301","sequence":"additional","affiliation":[{"name":"Universidad de Buenos Aires, Ciudad Universitaria , , Pab. II (1428) , ,","place":["Buenos Aires, Argentina"]},{"name":"Universidad de Buenos Aires, Ciudad Universitaria , , Pab. II (1428) , ,","place":["Buenos Aires, Argentina"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,9,19]]},"reference":[{"key":"2026090212505816500_cit1","doi-asserted-by":"crossref","first-page":"2764","DOI":"10.1016\/j.ccr.2011.04.012","article-title":"Nitroxyl\n(azanone) trapping by metalloporphyrins","volume":"255","author":"Doctorovich","year":"2011","journal-title":"Coord.\nChem. Rev."},{"key":"2026090212505816500_cit2","doi-asserted-by":"crossref","first-page":"7340","DOI":"10.1073\/pnas.112202099","article-title":"Nitroxyl\nand its anion in aqueous solutions: spin states,\nprotic equilibria, and reactivities toward oxygen and nitric oxide","volume":"99","author":"Shafirovich","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026090212505816500_cit3","doi-asserted-by":"crossref","first-page":"10463","DOI":"10.1073\/pnas.181191198","article-title":"Nitroxyl anion exerts\nredox-sensitive positive cardiac inotropy in vivo by calcitonin gene-related\npeptide signaling","volume":"98","author":"Paolocci","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.\nS. A."},{"key":"2026090212505816500_cit4","doi-asserted-by":"crossref","first-page":"14492","DOI":"10.1073\/pnas.93.25.14492","article-title":"NO from NO synthase","volume":"93","author":"Schmidt","year":"1996","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"key":"2026090212505816500_cit5","doi-asserted-by":"crossref","first-page":"12016","DOI":"10.1021\/ja3009693","article-title":"Chemical characterization\nof the smallest S-nitrosothiol, HSNO; cellular cross-talk\nof H2S and S-nitrosothiols","volume":"134","author":"Filipovic","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"2026090212505816500_cit6","doi-asserted-by":"crossref","first-page":"7982","DOI":"10.1021\/ja00312a031","article-title":"Metmyoglobin and methemoglobin as efficient traps for\nnitrosyl hydride (nitroxyl) in neutral aqueous solution","volume":"107","author":"Bazylinski","year":"1985","journal-title":"J. Am. Chem. Soc."},{"key":"2026090212505816500_cit7","doi-asserted-by":"crossref","first-page":"7986","DOI":"10.1021\/ja00312a032","article-title":"On the reaction of trioxodinitrate(II)\nwith hemoglobin and myoglobin","volume":"107","author":"Bazylinsky","year":"1985","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026090212505816500_cit8","doi-asserted-by":"crossref","first-page":"5018","DOI":"10.1021\/bi900122r","article-title":"Nitrosyl hydride (HNO) as an O2 analogue:\nLong-lived HNO adducts of ferrous globins","volume":"48","author":"Kumar","year":"2009","journal-title":"Biochemistry"},{"key":"2026090212505816500_cit9","doi-asserted-by":"crossref","first-page":"15272","DOI":"10.1021\/ja036370f","article-title":"Fast nitroxyl\ntrapping by ferric porphyrins","volume":"125","author":"Bari","year":"2003","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026090212505816500_cit10","doi-asserted-by":"crossref","first-page":"4680","DOI":"10.1021\/ja044632n","article-title":"Discrimination\nof nitroxyl and nitric oxide by water-soluble Mn(III) porphyrins","volume":"127","author":"Marti\u0301","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"2026090212505816500_cit11","doi-asserted-by":"crossref","first-page":"4673","DOI":"10.1016\/j.poly.2007.05.040","article-title":"HNO trapping and assisted decomposition of nitroxyl\ndonors by ferric hemes","volume":"26","author":"Sua\u0301rez","year":"2007","journal-title":"Polyhedron."},{"key":"2026090212505816500_cit12","doi-asserted-by":"crossref","first-page":"6955","DOI":"10.1021\/ic1007022","article-title":"A surface effect allows HNO\/NO discrimination\nby a\ncobalt porphyrin bound to gold","volume":"49","author":"Sua\u0301rez","year":"2010","journal-title":"Inorg. Chem."},{"key":"2026090212505816500_cit13","doi-asserted-by":"crossref","first-page":"8042","DOI":"10.1021\/ja0549906","article-title":"Mechanistic\nanalysis of reductive nitrosylation on\nwater-soluble cobalt(III)-porphyrins","volume":"128","author":"Roncaroli","year":"2006","journal-title":"J. Am.\nChem. Soc."},{"key":"2026090212505816500_cit14","doi-asserted-by":"crossref","first-page":"1044","DOI":"10.1016\/j.jinorgbio.2011.05.002","article-title":"A protective protein\nmatrix improves the discrimination\nof nitroxyl from nitric oxide by MnIII protoporphyrinate IX in aerobic\nmedia","volume":"105","author":"Boron","year":"2011","journal-title":"J. Inorg. Biochem."},{"key":"2026090212505816500_cit15","doi-asserted-by":"crossref","first-page":"10262","DOI":"10.1021\/ac402134b","article-title":"Time-resolved electrochemical quantification of azanone\n(HNO) at low nanomolar level","volume":"85","author":"Sua\u0301rez","year":"2013","journal-title":"Anal. Chem."},{"key":"2026090212505816500_cit16","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1016\/j.freeradbiomed.2011.02.008","article-title":"Detection of nitroxyl (HNO) by membrane\ninlet mass spectrometry","volume":"50","author":"Cline","year":"2011","journal-title":"Free Radical Biol.\nMed."},{"key":"2026090212505816500_cit17","doi-asserted-by":"crossref","first-page":"11675","DOI":"10.1021\/ja203652z","article-title":"Rapid and\nselective nitroxyl (HNO)\ntrapping by phosphines: kinetics and new aqueous ligations for HNO\ndetection and quantitation","volume":"133","author":"Reisz","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"2026090212505816500_cit18","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1016\/j.freeradbiomed.2008.04.036","article-title":"Generation of nitroxyl\nby heme protein-mediated peroxidation\nof hydroxylamine but not N-hydroxy-L-arginine","volume":"45","author":"Donzelli","year":"2008","journal-title":"Free Radical Biol. Med."},{"key":"2026090212505816500_cit19","doi-asserted-by":"crossref","first-page":"1247","DOI":"10.1021\/ac702024t","article-title":"Xerogel optical sensor films for\nquantitative detection of nitroxyl","volume":"80","author":"Dobmeier","year":"2008","journal-title":"Anal. Chem."},{"key":"2026090212505816500_cit20","doi-asserted-by":"crossref","first-page":"5536","DOI":"10.1021\/ja909148v","article-title":"Direct detection\nof nitroxyl in aqueous solution using\na tripodal copper(II) BODIPY complex","volume":"132","author":"Rosenthal","year":"2010","journal-title":"J. Am.\nChem. Soc."},{"key":"2026090212505816500_cit21","doi-asserted-by":"crossref","first-page":"2357","DOI":"10.1021\/ol103077q","article-title":"Visualization\nof nitroxyl in living cells by a chelated copper(II) coumarin complex","volume":"13","author":"Zhou","year":"2011","journal-title":"Org. Lett."},{"key":"2026090212505816500_cit22","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0741-8329(99)00056-7","article-title":"Reaction of nitroxyl,\nan aldehyde dehydrogenase inhibitor, with N-acetyl-L-cysteine","volume":"20","author":"Shoeman","year":"2000","journal-title":"Alcohol."},{"key":"2026090212505816500_cit23","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1006\/bbrc.1994.1668","article-title":"Bioassay discrimination between nitric oxide (NO.)\nand nitroxyl (NO-) using L-cysteine","volume":"201","author":"Pino","year":"1994","journal-title":"Biochem.\nBiophys. Res. Commun."},{"key":"2026090212505816500_cit24","doi-asserted-by":"crossref","first-page":"1056","DOI":"10.1016\/j.freeradbiomed.2005.10.058","article-title":"Discriminating formation\nof HNO from other reactive nitrogen oxide species","volume":"40","author":"Donzelli","year":"2006","journal-title":"Free Radical Biol. Med."},{"key":"2026090212505816500_cit25","doi-asserted-by":"crossref","first-page":"4625","DOI":"10.1016\/j.poly.2007.04.003","article-title":"Selective fluorescence detection\nof nitroxyl over nitric oxide in buffered aqueous solution using a\nconjugated metallopolymer","volume":"26","author":"Tennyson","year":"2006","journal-title":"Polyhedron"},{"key":"2026090212505816500_cit26","doi-asserted-by":"crossref","first-page":"8428","DOI":"10.1021\/ja101945j","article-title":"On the distinction\nbetween nitroxyl\nand nitric oxide using nitronyl nitroxides","volume":"132","author":"Samuni","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"2026090212505816500_cit27","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/S0010-8545(00)80259-3","article-title":"Principles of structure, bonding, and reactivity for\nmetal nitrosyl complexes","volume":"13","author":"Enemark","year":"1974","journal-title":"Coord. Chem. Rev."},{"key":"2026090212505816500_cit28","doi-asserted-by":"crossref","first-page":"12964","DOI":"10.1021\/ja9813764","article-title":"Electronic structure of reaction\nintermediate of cytochrome P450nor in its nitric oxide reduction","volume":"120","author":"Obayashi","year":"1998","journal-title":"J. Am. Chem. Soc."},{"key":"2026090212505816500_cit29","doi-asserted-by":"crossref","first-page":"5610","DOI":"10.1021\/ja00355a014","article-title":"Electrochemical and spectral characterization of iron\nmono- and dinitrosyl porphyrins","volume":"105","author":"Lancon","year":"1983","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026090212505816500_cit30","doi-asserted-by":"crossref","first-page":"1832","DOI":"10.1021\/ic00008a028","article-title":"Electrochemical\nand spectroscopic studies of iron porphyrin nitrosyls and their reduction\nproducts","volume":"30","author":"Choi","year":"1991","journal-title":"Inorg. Chem."},{"key":"2026090212505816500_cit31","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1007\/s00775-012-0893-0","article-title":"Reductive activation of the heme\niron-nitrosyl intermediate\nin the reaction mechanism of cytochrome c nitrite reductase: A theoretical\nstudy","volume":"17","author":"Bykov","year":"2012","journal-title":"J. Biol. Inorg. Chem."},{"key":"2026090212505816500_cit32","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1021\/ja905062w","article-title":"Successful\nstabilization of the elusive species {FeNO}8 in a heme\nmodel","volume":"132","author":"Pellegrino","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"2026090212505816500_cit33","doi-asserted-by":"crossref","first-page":"5138","DOI":"10.1021\/ja030645+","article-title":"Structural,\nspectroscopic, and computational\nstudy of an octahedral, non-heme [Fe-NO]6\u20138 Series:\n[Fe(NO)(cyclam-ac)]2+\/+\/0","volume":"126","author":"Serres","year":"2004","journal-title":"J. Am.\nChem. Soc."},{"key":"2026090212505816500_cit34","doi-asserted-by":"crossref","first-page":"12283","DOI":"10.1002\/anie.201305291","article-title":"Characterization\nof a high-spin non-heme {FeNO}(8)\ncomplex: implications for the reactivity of iron nitroxyl species\nin biology","volume":"52","author":"Speelman","year":"2013","journal-title":"Angew. Chem., Int. Ed."},{"key":"2026090212505816500_cit35","first-page":"7868","article-title":"Spectroelectrochemical\nevidence for the nitrosyl redox siblings NO+, NO*, and NO- coordinated\nto a strongly electron-accepting Fe(II) porphyrin: DFT calculations\nsuggest the presence of high-spin states after reduction of the Fe(II)-NO-\ncomplex","volume":"17","author":"Pellegrino","year":"2011","journal-title":"Chem.\u2500Eur. J."},{"key":"2026090212505816500_cit36","doi-asserted-by":"crossref","first-page":"1247","DOI":"10.1016\/j.jinorgbio.2004.04.005","article-title":"A nitrosyl\nhydride complex of a heme model [Ru(ttp)(HNO)(1-MeIm)]\n(ttp=tetratolylporphyrinato dianion)","volume":"98","author":"Lee","year":"2004","journal-title":"J. Inorg.\nBiochem."},{"key":"2026090212505816500_cit37","doi-asserted-by":"crossref","first-page":"2393","DOI":"10.1021\/ja994079n","article-title":"The HNO adduct of\nmyoglobin: Synthesis and characterization","volume":"122","author":"Lin","year":"2000","journal-title":"J.\nAm. Chem. Soc."},{"key":"2026090212505816500_cit38","doi-asserted-by":"crossref","first-page":"7766","DOI":"10.1021\/ic400977h","article-title":"Electronic\nstructure and biologically relevant reactivity of low-spin {FeNO}8 porphyrin model complexes: New insight from a bis-picket\nfence porphyrin","volume":"52","author":"Goodrich","year":"2013","journal-title":"Inorg. Chem."},{"key":"2026090212505816500_cit39","doi-asserted-by":"crossref","first-page":"4213","DOI":"10.1002\/anie.200806229","article-title":"Three redox states\nof nitrosyl: NO+, NO., and NO\u2013\/HNO interconvert reversibly\non the same pentacyanoferrate (II) platform","volume":"48","author":"Montenegro","year":"2009","journal-title":"Angew. Chem., Int. Ed."},{"key":"2026090212505816500_cit40","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1007\/s00726-010-0603-6","article-title":"Design of Mn porphyrins for treating\noxidative stress injuries and their redox-based regulation of cellular\ntranscriptional activities","volume":"42","author":"Batinic-Haberle","year":"2012","journal-title":"Amino Acids"},{"key":"2026090212505816500_cit41","doi-asserted-by":"crossref","first-page":"7351","DOI":"10.1021\/ic5007082","article-title":"Redox potential determines the reaction\nmechanism of HNO donors with Mn and Fe porphyrins: defining the better\ntraps","volume":"53","author":"A\u0301lvarez","year":"2014","journal-title":"Inorg. Chem."},{"key":"2026090212505816500_cit42","doi-asserted-by":"crossref","first-page":"3897","DOI":"10.1021\/bi00285a026","article-title":"Reaction of\nnitric oxide with heme proteins: Studies on metmyoglobin, opossum\nmethemoglobin, and microperoxidase","volume":"22","author":"Sharma","year":"1983","journal-title":"Biochemistry"},{"key":"2026090212505816500_cit43","doi-asserted-by":"crossref","first-page":"11614","DOI":"10.1021\/ja0113910","article-title":"Mechanistic studies\nof nitric oxide reactions with\nwater soluble iron(II), cobalt(II), and iron(III) porphyrin complexes\nin aqueous solutions: Implications for biological activity","volume":"123","author":"Laverman","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"2026090212505816500_cit44","doi-asserted-by":"crossref","first-page":"9196","DOI":"10.1073\/pnas.1430507100","article-title":"A biochemical rationale for the discrete\nbehavior of nitroxyl and nitric oxide in the cardiovascular system","volume":"100","author":"Miranda","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026090212505816500_cit45","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1021\/ja0376184","article-title":"Efficient trapping\nof HNO by deoxymyoglobin","volume":"126","author":"Sulc","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"2026090212505816500_cit46","doi-asserted-by":"crossref","first-page":"5177","DOI":"10.1074\/jbc.M008282200","article-title":"Mapping\npathways for O2 entry and\nexit from myoglobin","volume":"276","author":"Scott","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2026090212505816500_cit47","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.jinorgbio.2012.10.008","article-title":"The pH of\nHNO donation is modulated by ring substituents in Piloty\u2019s\nacid derivatives: Azanone donors at biological pH","volume":"118","author":"Sirsalmath","year":"2013","journal-title":"J. Inorg. Biochem."},{"key":"2026090212505816500_cit48","doi-asserted-by":"crossref","first-page":"4007","DOI":"10.1021\/ja312092x","article-title":"Nitrite reduction\nmediated by heme models. Routes to NO and HNO?","volume":"135","author":"Heinecke","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"2026090212505816500_cit49","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1021\/jm3012036","article-title":"Beyond H2S\nand NO Interplay: Hydrogen Sulfide and Nitroprusside React Directly\nto Give Nitroxyl (HNO). A New Pharmacological Source of HNO","volume":"56","author":"Filipovic","year":"2013","journal-title":"J. Med. Chem."},{"key":"2026090212505816500_cit50","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms5381","article-title":"H2S and\nNO generate nitroxyl and activate HNO-trpa1-CGRP pathway for neurovascular\ncontrol","volume":"5","author":"Eberhardt","year":"2014","journal-title":"Nat. Commun."},{"key":"2026090212505816500_cit51","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.ccr.2009.07.021","article-title":"Mechanistic studies\nof nitrite reactions with metalloproteins\nand models relevant to mammalian physiology","volume":"254","author":"Heinecke","year":"2010","journal-title":"Coord. Chem. Rev."},{"key":"2026090212505816500_cit52","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.jinorgbio.2012.09.022","article-title":"Synthesis and characterization\nof lithium oxonitrate (LiNO)","volume":"118","author":"Switzer","year":"2013","journal-title":"J. Inorg. Biochem."},{"key":"2026090212505816500_cit53","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.jinorgbio.2012.08.027","article-title":"A comparison\nof the chemistry associated\nwith the biological signaling and actions of nitroxyl (HNO) and nitric\noxide (NO)","volume":"118","author":"Fukuto","year":"2013","journal-title":"J. Inorg. Biochem."},{"key":"2026090212505816500_cit54","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1021\/ar400256u","article-title":"Heme versus non-heme\niron-nitroxyl {FeN(H)O}8 complexes: electronic structure\nand biologically relevant reactivity","volume":"47","author":"Speelman","year":"2014","journal-title":"Acc. Chem.\nRes."}],"container-title":["Accounts of Chemical Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/ar500153c","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/achre4\/article-pdf\/47\/10\/2907\/12048538\/ar500153c.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/achre4\/article-pdf\/47\/10\/2907\/12048538\/ar500153c.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T16:51:08Z","timestamp":1788367868000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/achre4\/article\/47\/10\/2907\/1248065\/Reactions-of-HNO-with-Metal-Porphyrins"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,9,19]]},"references-count":54,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2014,9,19]]},"published-print":{"date-parts":[[2014,10,21]]}},"URL":"https:\/\/doi.org\/10.1021\/ar500153c","relation":{},"ISSN":["0001-4842","1520-4898"],"issn-type":[{"value":"0001-4842","type":"print"},{"value":"1520-4898","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,9,19]]}}}