{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T01:04:57Z","timestamp":1788915897836,"version":"build-2803163510"},"reference-count":148,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,9,22]],"date-time":"2024-09-22T00:00:00Z","timestamp":1726963200000},"content-version":"am","delay-in-days":296,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100009404","name":"MIRA Institute, University of Twente","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100009404","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35GM139536"],"award-info":[{"award-number":["R35GM139536"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Inorganic Biochemistry"],"published-print":{"date-parts":[[2023,12]]},"DOI":"10.1016\/j.jinorgbio.2023.112367","type":"journal-article","created":{"date-parts":[[2023,9,9]],"date-time":"2023-09-09T05:30:05Z","timestamp":1694237405000},"page":"112367","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":14,"special_numbering":"C","title":["Heme-copper and Heme O2-derived synthetic (bioinorganic) chemistry toward an understanding of cytochrome c oxidase dioxygen chemistry"],"prefix":"10.1016","volume":"249","author":[{"given":"Sanjib","family":"Panda","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hai","family":"Phan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kenneth D.","family":"Karlin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jinorgbio.2023.112367_bb0005","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1021\/cr500266a","article-title":"Reaction mechanism of cytochrome c oxidase","volume":"115","author":"Yoshikawa","year":"2015","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0010","doi-asserted-by":"crossref","first-page":"2469","DOI":"10.1021\/acs.chemrev.7b00664","article-title":"Oxygen activation and energy conservation by cytochrome c oxidase","volume":"118","author":"Wikstr\u00f6m","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0015","doi-asserted-by":"crossref","first-page":"10840","DOI":"10.1021\/acs.chemrev.8b00074","article-title":"Synthetic Fe\/Cu complexes: toward understanding Heme-copper oxidase structure and function","volume":"118","author":"Adam","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0020","doi-asserted-by":"crossref","first-page":"2439","DOI":"10.1021\/cr0680639","article-title":"Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis","volume":"108","author":"Cracknell","year":"2008","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0025","doi-asserted-by":"crossref","first-page":"10068","DOI":"10.1021\/jacs.9b04271","article-title":"Geometric and electronic structure contributions to O\u2013O cleavage and the resultant intermediate generated in Heme-Copper oxidases","volume":"141","author":"Schaefer","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0030","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1038\/376660a0","article-title":"Structure at 2.8 \u00c5 resolution of cytochrome c oxidase from Paracoccus denitrificans","volume":"376","author":"Iwata","year":"1995","journal-title":"Nature"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0035","doi-asserted-by":"crossref","first-page":"1136","DOI":"10.1126\/science.272.5265.1136","article-title":"The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 \u00c5","volume":"272","author":"Tsukihara","year":"1996","journal-title":"Science"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0040","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fchem.2023.1108190","article-title":"Recent progress in experimental studies on the catalytic mechanism of cytochrome c oxidase","volume":"11","author":"Shimada","year":"2023","journal-title":"Front. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0045","doi-asserted-by":"crossref","first-page":"23882","DOI":"10.1074\/jbc.M115.711770","article-title":"The Mg2+\u2212containing water cluster of mammalian cytochrome c oxidase collects four pumping proton equivalents in each catalytic cycle","volume":"291","author":"Yano","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0050","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.1126\/science.abh3209","article-title":"The three-spin intermediate at the O-O cleavage and proton-pumping junction in heme-cu oxidases","volume":"373","author":"Jose","year":"2021","journal-title":"Science"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0055","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1021\/acs.biochem.5b01205","article-title":"Mechanism of oxygen reduction in cytochrome c oxidase and the role of the active site tyrosine","volume":"55","author":"Blomberg","year":"2016","journal-title":"Biochem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0060","doi-asserted-by":"crossref","first-page":"16844","DOI":"10.1073\/pnas.1220379110","article-title":"Computational study of the activated OH state in the catalytic mechanism of cytochrome c oxidase","volume":"110","author":"Sharma","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0065","doi-asserted-by":"crossref","first-page":"20261","DOI":"10.1074\/jbc.M113.468488","article-title":"The protein effect in the structure of two Ferryl-Oxo intermediates at the same oxidation level in the Heme copper binuclear center of cytochrome c oxidase","volume":"288","author":"Pinakoulaki","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0070","first-page":"813","article-title":"Stabilization of the peroxy intermediate in the oxygen splitting reaction of cytochrome cbb3","volume":"2011","author":"Sharma","year":"1807","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0075","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.febslet.2004.06.036","article-title":"The intrinsic stability of the second intermediate following the dioxygen-bound form in the O2 reduction by cytochrome c oxidase","volume":"570","author":"Oda","year":"2004","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0080","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.1700279","article-title":"Splitting of the O-O bond at the heme-copper catalytic site of respiratory oxidases","volume":"3","author":"Poiana","year":"2017","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0085","doi-asserted-by":"crossref","first-page":"5231","DOI":"10.1021\/ic034060s","article-title":"A metal-bridging mechanism for O-O bond cleavage in cytochrome c oxidase","volume":"42","author":"Blomberg","year":"2003","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0090","first-page":"1295","article-title":"Radical formation in cytochrome c oxidase","volume":"2011","author":"Yu","year":"1807","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0095","doi-asserted-by":"crossref","first-page":"31580","DOI":"10.1074\/jbc.M705520200","article-title":"Kinetic resolution of a tryptophan-radical intermediate in the reaction cycle of Paracoccus denitrificans cytochrome c oxidase","volume":"282","author":"Wiertz","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0100","first-page":"579","article-title":"Structural studies on bovine heart cytochrome c oxidase","volume":"2012","author":"Yoshikawa","year":"1817","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0105","doi-asserted-by":"crossref","first-page":"3572","DOI":"10.1073\/pnas.1814526116","article-title":"Snapshot of an oxygen intermediate in the catalytic reaction of cytochrome c oxidase","volume":"116","author":"Ishigami","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0110","doi-asserted-by":"crossref","first-page":"18761","DOI":"10.1074\/jbc.M211925200","article-title":"Direct detection of Fe(IV)=O intermediates in the cytochrome aa3 oxidase from Paracoccus denitrificans\/H2O2 reaction","volume":"278","author":"Pinakoulaki","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0115","doi-asserted-by":"crossref","first-page":"7389","DOI":"10.1021\/ja00311a029","article-title":"Mechanism of cytochrome c oxidase-catalyzed dioxygen reduction at low temperatures. Evidence for two intermediates at the three-electron level and entropic promotion of the bond-breaking step","volume":"107","author":"Blair","year":"1985","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0120","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1021\/ar700031t","article-title":"Heme-copper\/dioxygen adduct formation, properties, and reactivity","volume":"40","author":"Chuf\u00e1n","year":"2007","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0125","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1021\/cr0206162","article-title":"Synthetic models for Heme-copper oxidases","volume":"104","author":"Kim","year":"2004","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0130","doi-asserted-by":"crossref","first-page":"2462","DOI":"10.1021\/acs.accounts.5b00265","article-title":"Synthetic Heme\/copper assemblies: toward an understanding of cytochrome c oxidase interactions with dioxygen and nitrogen oxides","volume":"48","author":"Hematian","year":"2015","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0135","doi-asserted-by":"crossref","first-page":"5065","DOI":"10.1039\/b808070b","article-title":"Functional biomimetic models for the active site in the respiratory enzyme cytochrome c oxidase","author":"Collman","year":"2008","journal-title":"Chem. Commun."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0140","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1021\/cr0206059","article-title":"Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin","volume":"104","author":"Collman","year":"2004","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0145","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1126\/science.1135844","article-title":"A cytochrome c oxidase model catalyzes oxygen to water reduction under rate-limiting electron flux","volume":"315","author":"Collman","year":"2007","journal-title":"Science"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0150","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1126\/science.275.5302.949","article-title":"A functional model related to cytochrome c oxidase and its electrocatalytic four-electron reduction of O2","volume":"275","author":"Collman","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0155","doi-asserted-by":"crossref","first-page":"1291","DOI":"10.1039\/b901972n","article-title":"Electrochemical applications. How click chemistry brought biomimetic models to the next level: electrocatalysis under controlled rate of electron transfer","volume":"39","author":"Decreau","year":"2010","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0160","doi-asserted-by":"crossref","DOI":"10.3389\/fphys.2015.00210","article-title":"Three toxic gases meet in the mitochondria","volume":"6","author":"Decreau","year":"2015","journal-title":"Front. Physiol."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0165","doi-asserted-by":"crossref","first-page":"14560","DOI":"10.1021\/ja061507y","article-title":"Characterization of the Phenoxyl radical in model complexes for the CuB site of cytochrome c oxidase: steady-state and transient absorption measurements, UV resonance Raman spectroscopy, EPR spectroscopy, and DFT calculations for M-BIAIP","volume":"128","author":"Nagano","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0170","doi-asserted-by":"crossref","first-page":"1836","DOI":"10.1002\/anie.200462582","article-title":"A functional model of the cytochrome c oxidase active site: unique conversion of a heme-m-peroxo-CuII intermediate into heme-superoxo\/CuI","volume":"44","author":"Liu","year":"2005","journal-title":"Angew. Chem. Int. Ed. Eng."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0175","doi-asserted-by":"crossref","first-page":"2788","DOI":"10.1002\/anie.200351415","article-title":"Isolation and crystal structure of a Peroxo-bridged Heme-copper complex","volume":"42","author":"Chishiro","year":"2003","journal-title":"Angew. Chem. Int. Ed. Eng."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0180","doi-asserted-by":"crossref","first-page":"2486","DOI":"10.1039\/D0CS01297A","article-title":"Molecular understanding of heteronuclear active sites in heme\u2013copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling","volume":"50","author":"Reed","year":"2021","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0185","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1002\/ijch.201600033","article-title":"Using biosynthetic models of Heme-copper oxidase and nitric oxide reductase in myoglobin to elucidate structural features responsible for enzymatic activities","volume":"56","author":"Bhagi-Damodaran","year":"2016","journal-title":"Isr. J. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0190","doi-asserted-by":"crossref","first-page":"5020","DOI":"10.1039\/C5CS00923E","article-title":"Design and engineering of artificial oxygen-activating metalloenzymes","volume":"45","author":"Nastri","year":"2016","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0195","doi-asserted-by":"crossref","first-page":"2356","DOI":"10.1021\/acscatal.0c04753","article-title":"Impact of Heterometallic cooperativity of Iron and copper active sites on Electrocatalytic oxygen reduction kinetics","volume":"11","author":"Kato","year":"2021","journal-title":"ACS Catal."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0200","doi-asserted-by":"crossref","first-page":"12897","DOI":"10.1021\/jacs.5b06513","article-title":"Electrocatalytic O2-reduction by synthetic cytochrome c oxidase mimics: identification of a \u201cbridging Peroxo\u201d intermediate involved in facile 4e\u2013\/4H+ O2-reduction","volume":"137","author":"Chatterjee","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0205","doi-asserted-by":"crossref","first-page":"1989","DOI":"10.1039\/C7SC04732K","article-title":"A water-soluble supramolecular complex that mimics the heme\/copper hetero-binuclear site of cytochrome c oxidase","volume":"9","author":"Kitagishi","year":"2018","journal-title":"Chem. Sci."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0210","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.poly.2013.01.050","article-title":"CO and O2 binding studies of new model complexes for CcO","volume":"54","author":"Ladomenou","year":"2013","journal-title":"Polyhedron"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0215","doi-asserted-by":"crossref","first-page":"6183","DOI":"10.1021\/ja010602y","article-title":"Dioxygen reactivity of mononuclear Heme and copper components yielding a high-spin Heme-Peroxo-Cu complex","volume":"123","author":"Ghiladi","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0220","doi-asserted-by":"crossref","first-page":"3889","DOI":"10.1021\/ic061726k","article-title":"Further insights into the spectroscopic properties, electronic structure, and kinetics of formation of the Heme-Peroxo-copper complex [(F8TPP)FeIII-(O22\u2212)-CuII(TMPA)]+","volume":"46","author":"Ghiladi","year":"2007","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0225","doi-asserted-by":"crossref","first-page":"3629","DOI":"10.1021\/ic9020993","article-title":"Heme-copper-dioxygen complexes: toward understanding ligand-environmental effects on the coordination geometry, electronic structure, and reactivity","volume":"49","author":"Halime","year":"2010","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0230","doi-asserted-by":"crossref","first-page":"9783","DOI":"10.1021\/ja00100a067","article-title":"A synthetic analogue for the oxygen binding site in cytochrome c oxidase","volume":"116","author":"Collman","year":"1994","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0235","doi-asserted-by":"crossref","first-page":"3017","DOI":"10.1021\/ic061686k","article-title":"Generation and characterization of [(P)M-(X)-Co(TMPA)]n+ assemblies; P = Porphyrinate, M = FeIII and CoIII, X = O2\u2212, OH\u2212, O22\u2212, and TMPA = Tris(2-pyridylmethyl)amine","volume":"46","author":"Chuf\u00e1n","year":"2007","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0240","doi-asserted-by":"crossref","first-page":"4170","DOI":"10.1021\/ja0125265","article-title":"Contrasting copper-dioxygen chemistry arising from alike tridentate Alkyltriamine copper(I) complexes","volume":"124","author":"Liang","year":"2002","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0245","doi-asserted-by":"crossref","first-page":"8513","DOI":"10.1021\/ja300674m","article-title":"Geometric and electronic structure of [{Cu(MeAN)}2(\u03bc-\u03b72:\u03b72(O22\u2212))]2+ with an unusually Long O\u2013O Bond: O\u2013O bond weakening vs activation for reductive cleavage","volume":"134","author":"Park","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0250","doi-asserted-by":"crossref","first-page":"3246","DOI":"10.1021\/ja00009a005","article-title":"An electronic structural comparison of copper-peroxide complexes of relevance to hemocyanin and tyrosinase active sites","volume":"113","author":"Ross","year":"1991","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0255","doi-asserted-by":"crossref","first-page":"4570","DOI":"10.1002\/1521-3773(20011217)40:24<4570::AID-ANIE4570>3.0.CO;2-4","article-title":"Oxygen binding, activation, and reduction to water by copper proteins","volume":"40","author":"Solomon","year":"2001","journal-title":"Angew. Chem. Int. Ed. Eng."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0260","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1002\/anie.201104080","article-title":"Spectroscopic elucidation of a new Heme\/copper dioxygen structure type: implications for O...O bond rupture in cytochrome\u00a0c oxidase","volume":"51","author":"Kieber-Emmons","year":"2012","journal-title":"Angew. Chem. Int. Ed. Eng."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0265","doi-asserted-by":"crossref","first-page":"2893","DOI":"10.1039\/C8SC05165H","article-title":"Influence of intramolecular secondary sphere hydrogen-bonding interactions on cytochrome c oxidase inspired low-spin Heme-Peroxo-copper complexes","volume":"10","author":"Ehudin","year":"2019","journal-title":"Chem. Sci."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0270","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1021\/ja5115198","article-title":"A \u201cnaked\u201d FeIII-(O22-)-CuII Species allows for structural and spectroscopic tuning of low-spin Heme-Peroxo-Cu complexes","volume":"137","author":"Garcia-Bosch","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0275","doi-asserted-by":"crossref","first-page":"3623","DOI":"10.1073\/pnas.0737180100","article-title":"Superoxo, mu-peroxo and mu-oxo complexes from heme\/O2 and heme-copper\/O2 reactivity studies: copper-ligand influences in cytochrome c oxidase models","volume":"100","author":"Kim","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0280","doi-asserted-by":"crossref","first-page":"11777","DOI":"10.1021\/ic2018727","article-title":"Electronic structure of a low-spin Heme\/cu peroxide complex: spin-state and spin-topology contributions to reactivity","volume":"50","author":"Kieber-Emmons","year":"2011","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0285","doi-asserted-by":"crossref","first-page":"7958","DOI":"10.1021\/jacs.7b03292","article-title":"Phenol-induced O\u2013O bond cleavage in a low-spin Heme\u2013Peroxo\u2013Copper complex: implications for O2 reduction in Heme\u2013Copper oxidases","volume":"139","author":"Schaefer","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0290","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1021\/jacs.6b11322","article-title":"Critical aspects of Heme\u2013Peroxo\u2013Cu complex structure and nature of proton source dictate Metal\u2013Operoxo breakage versus reductive O\u2013O cleavage chemistry","volume":"139","author":"Adam","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0295","doi-asserted-by":"crossref","first-page":"2403","DOI":"10.1021\/ja993774s","article-title":"Insights into the functional role of the tyrosine-histidine linkage in cytochrome c oxidase","volume":"122","author":"McCauley","year":"2000","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0300","doi-asserted-by":"crossref","first-page":"12802","DOI":"10.1021\/ja011450+","article-title":"Electronic structure of the high-spin Iron(III)-Alkylperoxo complexes and its relation to low-spin analogues: reaction coordinate of O-O bond Homolysis","volume":"123","author":"Lehnert","year":"2001","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0305","doi-asserted-by":"crossref","first-page":"11027","DOI":"10.1021\/ja029380+","article-title":"Oxidation mechanism of phenols by dicopper-dioxygen (Cu2O2) complexes","volume":"125","author":"Osako","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0310","doi-asserted-by":"crossref","first-page":"6961","DOI":"10.1021\/cr100085k","article-title":"Thermochemistry of proton-coupled Electron transfer reagents and its implications","volume":"110","author":"Warren","year":"2010","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0315","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.1590\/S0103-50532012005000007","article-title":"Anionic chromogenic chemosensors highly selective for fluoride or cyanide based on 4-(4-Nitrobenzylideneamine)phenol","volume":"23","author":"Nicoleti","year":"2012","journal-title":"J. Braz. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0320","doi-asserted-by":"crossref","first-page":"4838","DOI":"10.1021\/ic980606c","article-title":"Effect of protonation on Peroxo-copper bonding: spectroscopic and electronic structure study of [Cu2(UN-O\u2212)(OOH)]2+","volume":"37","author":"Root","year":"1998","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0325","series-title":"The Properties of Metal-Porphyrin and Similar Complexes","first-page":"359","author":"Braterman","year":"2007"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0330","doi-asserted-by":"crossref","first-page":"5725","DOI":"10.1021\/ic0496572","article-title":"Steric and hydrogen-bonding effects on the stability of copper complexes with small molecules","volume":"43","author":"Wada","year":"2004","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0335","doi-asserted-by":"crossref","first-page":"4378","DOI":"10.1002\/ejic.200300178","article-title":"Thermal stability and absorption spectroscopic behavior of (mu-Peroxo)dicopper complexes regulated with intramolecular hydrogen bonding interactions","author":"Yamaguchi","year":"2003","journal-title":"Eur. J. Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0340","doi-asserted-by":"crossref","first-page":"1702","DOI":"10.1021\/ja110466q","article-title":"Cupric superoxo-mediated intermolecular C\u2013H activation chemistry","volume":"133","author":"Peterson","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0345","doi-asserted-by":"crossref","first-page":"9042","DOI":"10.1021\/jacs.8b04671","article-title":"Intramolecular hydrogen bonding enhances stability and reactivity of mononuclear cupric superoxide complexes","volume":"140","author":"Bhadra","year":"2018","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0350","doi-asserted-by":"crossref","first-page":"4936","DOI":"10.1021\/jacs.9b00118","article-title":"Spin interconversion of Heme-Peroxo-copper complexes facilitated by intramolecular hydrogen-bonding interactions","volume":"141","author":"Schaefer","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0355","doi-asserted-by":"crossref","first-page":"1238","DOI":"10.1021\/ic048907b","article-title":"Dioxygen reactivity of copper and heme-copper complexes possessing an imidazole-phenol cross-link","volume":"44","author":"Kim","year":"2005","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0360","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S0009-2614(03)00683-3","article-title":"Theoretical study of role of H2O molecule on initial stage of reduction of O2 molecule in active site of cytochrome c oxidase","volume":"374","author":"Yoshioka","year":"2003","journal-title":"Chem. Phys. Lett."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0365","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.1021\/acs.chemrev.7b00373","article-title":"Oxygen activation and radical transformations in Heme proteins and Metalloporphyrins","volume":"118","author":"Huang","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0370","doi-asserted-by":"crossref","first-page":"4119","DOI":"10.1039\/c1cs15046d","article-title":"Structure:function relationships in molecular spin-crossover complexes","volume":"40","author":"Halcrow","year":"2011","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0375","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1039\/b003504l","article-title":"Spin crossover phenomena in Fe(II) complexes","volume":"29","author":"Gutlich","year":"2000","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0380","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1021\/ja045719b","article-title":"EPR and optical spectroscopic studies of Met80X mutants of yeast ferricytochrome c. models for intermediates in the alkaline transition","volume":"127","author":"Silkstone","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0385","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/0005-2795(69)90096-8","article-title":"Analysis of thermal equilibrium between high-spin and low-spin states in ferrihemoglobin complexes","volume":"194","author":"Iizuka","year":"1969","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0390","doi-asserted-by":"crossref","first-page":"11923","DOI":"10.1021\/ja026179q","article-title":"Functional analogues of the dioxygen reduction site in cytochrome oxidase: mechanistic aspects and possible effects of CuB","volume":"124","author":"Boulatov","year":"2002","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0395","doi-asserted-by":"crossref","first-page":"3755","DOI":"10.1021\/jp400260u","article-title":"Effect of distal interactions on O2 binding to heme","volume":"117","author":"Kepp","year":"2013","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0400","doi-asserted-by":"crossref","first-page":"2253","DOI":"10.1021\/cr0307143","article-title":"Structure and chemistry of cytochrome P450","volume":"105","author":"Denisov","year":"2005","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0405","doi-asserted-by":"crossref","first-page":"4796","DOI":"10.1002\/anie.201411399","article-title":"Hydrogen-bonding interactions trigger a spin-flip in iron(III) porphyrin complexes","volume":"54","author":"Sahoo","year":"2015","journal-title":"Angew. Chem. Int. Ed. Eng."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0410","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.jinorgbio.2015.11.013","article-title":"Second sphere control of spin state: differential tuning of axial ligand bonds in ferric porphyrin complexes by hydrogen bonding","volume":"155","author":"Mittra","year":"2016","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0415","doi-asserted-by":"crossref","first-page":"4753","DOI":"10.1021\/ja210535w","article-title":"Two Tyrosyl radicals stabilize high oxidation states in cytochrome c oxidase for efficient energy conservation and proton translocation","volume":"134","author":"Yu","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0420","doi-asserted-by":"crossref","first-page":"4469","DOI":"10.1021\/ja209985v","article-title":"Formation of Iron(III) meso-Chloro-isoporphyrin as a reactive chlorinating agent from Oxoiron(IV) porphyrin pi-cation radical","volume":"134","author":"Cong","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0425","doi-asserted-by":"crossref","first-page":"11784","DOI":"10.1021\/ja00078a017","article-title":"Preparation, characterization, and reactions of novel iron(III) porphyrin dication complexes","volume":"115","author":"Tsurumaki","year":"1993","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0430","doi-asserted-by":"crossref","first-page":"3451","DOI":"10.1021\/ja00714a038","article-title":"Pi-cation radicals and dications of metalloporphyrins","volume":"92","author":"Fajer","year":"1970","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0435","doi-asserted-by":"crossref","first-page":"10632","DOI":"10.1021\/jacs.9b01791","article-title":"Formation and reactivity of new Isoporphyrins: implications for understanding the Tyr-his cross-link cofactor biogenesis in cytochrome c oxidase","volume":"141","author":"Ehudin","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0440","unstructured":"P. R. Ortiz de Montellano, Ed., Cytochrome P-450. Structure, Mechanism, and Biochemistry; Kluwer Academic \/ Plenum Publishers: New York, 2005."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0445","doi-asserted-by":"crossref","first-page":"2841","DOI":"10.1021\/cr9500500","article-title":"Heme containing Oxygenases","volume":"96","author":"Sono","year":"1996","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0450","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1126\/science.1193478","article-title":"Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics","volume":"330","author":"Rittle","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0455","doi-asserted-by":"crossref","first-page":"2231","DOI":"10.1021\/bi7023817","article-title":"Revisiting Heme mechanisms. A perspective on the mechanisms of Nitric Oxide Synthase (NOS), Heme Oxygenase (HO), and Cytochrome P450s (CYP450s)","volume":"47","author":"Zhu","year":"2008","journal-title":"Biochem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0460","series-title":"The Handbook of Porphyrin Science","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1142\/9789814322386_0015","article-title":"The role of Heme-Nitrosyls in the biosynthesis, transport, sensing, and detoxification of nitric oxide (NO) in biological systems: Enzymes and model complexes","author":"Lehnert","year":"2011"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0465","doi-asserted-by":"crossref","first-page":"1402","DOI":"10.1021\/ja067209i","article-title":"Distinct reaction pathways followed upon reduction of oxy-Heme oxygenase and oxy-myoglobin as characterized by M\u00f6ssbauer spectroscopy","volume":"129","author":"Garcia-Serres","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0470","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1021\/ar9001685","article-title":"Heme oxygenase reveals its strategy for catalyzing three successive oxygenation reactions","volume":"43","author":"Matsui","year":"2010","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0475","doi-asserted-by":"crossref","first-page":"3779","DOI":"10.1073\/pnas.1523333113","article-title":"Unique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation","volume":"113","author":"Matsui","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0480","doi-asserted-by":"crossref","first-page":"3919","DOI":"10.1021\/cr400415k","article-title":"Heme enzyme structure and function","volume":"114","author":"Poulos","year":"2014","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0485","doi-asserted-by":"crossref","first-page":"3686","DOI":"10.1073\/pnas.1503340112","article-title":"Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive","volume":"112","author":"Wang","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0490","doi-asserted-by":"crossref","first-page":"3104","DOI":"10.1021\/jacs.9b12571","article-title":"Heme-FeIII superoxide, peroxide and Hydroperoxide thermodynamic relationships: FeIII-O2\u2022\u2013 complex H-atom abstraction reactivity","volume":"142","author":"Kim","year":"2020","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0495","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.abb.2010.09.013","article-title":"Active intermediates in heme monooxygenase reactions as revealed by cryoreduction\/annealing, EPR\/ENDOR studies","volume":"507","author":"Davydov","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0500","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1021\/ar0202565","article-title":"ENDOR of metalloenzymes","volume":"36","author":"Hoffman","year":"2003","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0505","doi-asserted-by":"crossref","first-page":"5907","DOI":"10.1002\/anie.202013791","article-title":"Ferric Heme superoxide reductive transformations to ferric Heme (hydro)peroxide species: spectroscopic characterization and thermodynamic implications for H-atom transfer (HAT)","volume":"60","author":"Kim","year":"2021","journal-title":"Angew. Chem. Int. Ed. Eng."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0510","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1021\/ja00839a026","article-title":"Picket fence porphyrins. Synthetic models for oxygen binding hemoproteins","volume":"97","author":"Collman","year":"1975","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0515","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1073\/pnas.71.4.1326","article-title":"Structure of an Iron(II) dioxygen complex; a model for oxygen carrying hemeproteins","volume":"71","author":"Collman","year":"1974","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0520","doi-asserted-by":"crossref","first-page":"2008","DOI":"10.1021\/ja953694y","article-title":"The diverse reactivity of Peroxy ferric porphyrin complexes of electron-rich and electron-poor porphyrins","volume":"118","author":"Selke","year":"1996","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0525","doi-asserted-by":"crossref","first-page":"4268","DOI":"10.1021\/ja00532a053","article-title":"Reactions of superoxide with Iron porphyrins in aprotic-solvents - a high-spin ferric porphyrin Peroxo complex","volume":"102","author":"McCandlish","year":"1980","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0530","doi-asserted-by":"crossref","first-page":"3672","DOI":"10.1021\/ja1001955","article-title":"Formation of an end-on ferric Peroxo intermediate upon one-electron reduction of a ferric Superoxo Heme","volume":"132","author":"Liu","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0535","doi-asserted-by":"crossref","first-page":"8872","DOI":"10.1039\/D1SC01952J","article-title":"Proton-coupled electron transfer reactivities of electronically divergent heme superoxide intermediates: a kinetic, thermodynamic, and theoretical study","volume":"12","author":"Mondal","year":"2021","journal-title":"Chem. Sci."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0540","doi-asserted-by":"crossref","first-page":"1675","DOI":"10.1021\/ja046939s","article-title":"Synthesis, structure determination, and spectroscopic\/computational characterization of a series of Fe(II)-thiolate model complexes: implications for Fe-S bonding in superoxide reductases","volume":"127","author":"Fiedler","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0545","doi-asserted-by":"crossref","first-page":"10704","DOI":"10.1021\/ic3016035","article-title":"EPR, resonance Raman, and DFT calculations on thiolate- and imidazole-bound Iron(III) porphyrin complexes: role of the axial ligand in tuning the electronic structure","volume":"51","author":"Das","year":"2012","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0550","doi-asserted-by":"crossref","first-page":"7336","DOI":"10.1002\/anie.201502367","article-title":"Characterization of mononuclear non-heme Iron(III)-Superoxo complex with a five-azole ligand set","volume":"54","author":"Oddon","year":"2015","journal-title":"Angew. Chem. Int. Ed. Eng."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0555","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1002\/chem.200390096","article-title":"Iron twin-coronet porphyrins as models of myoglobin and hemoglobin: Amphibious electrostatic effects of overhanging hydroxyl groups for successful CO\/O2 discrimination","volume":"9","author":"Tani","year":"2003","journal-title":"Chem Eur J"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0560","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1073\/pnas.98.2.479","article-title":"Simultaneous observation of the O---O and Fe---O2 stretching modes in oxyhemoglobins","volume":"98","author":"Das","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0565","doi-asserted-by":"crossref","first-page":"9262","DOI":"10.1002\/anie.200904572","article-title":"Spectroscopic characterization of a Hydroperoxo-Heme intermediate: conversion of a side-on Peroxo to an end-on Hydroperoxo complex","volume":"48","author":"Liu","year":"2009","journal-title":"Angew. Chem. Int. Ed. Eng."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0570","doi-asserted-by":"crossref","first-page":"2639","DOI":"10.1021\/ic034065p","article-title":"End-on and side-on peroxo derivatives of non-Heme Iron complexes with pentadentate ligands: models for putative intermediates in biological Iron\/dioxygen chemistry","volume":"42","author":"Roelfes","year":"2003","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0575","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/j.ccr.2012.05.009","article-title":"Resonance Raman characterization of mononuclear heme-peroxo intermediate models","volume":"257","author":"Ohta","year":"2013","journal-title":"Coord. Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0580","doi-asserted-by":"crossref","first-page":"4150","DOI":"10.1002\/anie.200900118","article-title":"Structural characterization and remarkable axial ligand effect on the nucleophilic reactivity of a Nonheme manganese(III)-Peroxo complex","volume":"48","author":"Annaraj","year":"2009","journal-title":"Angew. Chem. Int. Ed. Eng."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0585","doi-asserted-by":"crossref","first-page":"7869","DOI":"10.1021\/ja901868q","article-title":"S K-edge XAS and DFT calculations on cytochrome P450: covalent and ionic contributions to the cysteine-Fe bond and their contribution to reactivity","volume":"131","author":"Dey","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0590","doi-asserted-by":"crossref","first-page":"7323","DOI":"10.1021\/acs.joc.7b02547","article-title":"Structural effects on the pH-dependent redox properties of organic Nitroxyls: Pourbaix diagrams for TEMPO, ABNO, and three TEMPO analogs","volume":"83","author":"Gerken","year":"2018","journal-title":"J. Organomet. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0595","doi-asserted-by":"crossref","first-page":"5444","DOI":"10.1021\/ja111376n","article-title":"Can ferric-superoxide act as a potential oxidant in P450cam? QM\/MM investigation of hydroxylation, epoxidation, and sulfoxidation","volume":"133","author":"Lai","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0600","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1038\/nchem.1855","article-title":"Enzymatic C-H bond activation: using push to get pull","volume":"6","author":"Groves","year":"2014","journal-title":"Nat. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0605","doi-asserted-by":"crossref","first-page":"16016","DOI":"10.1021\/jacs.6b09693","article-title":"Spectroscopic investigations of catalase compound II: characterization of an Iron(IV) hydroxide intermediate in a non-thiolate-ligated Heme enzyme","volume":"138","author":"Yosca","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0610","series-title":"Direct Visualization of a Fe(IV)\u2013OH Intermediate in a Heme Enzyme","first-page":"13445","volume":"7","author":"Kwon","year":"2016"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0615","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1021\/acs.accounts.7b00463","article-title":"The nature and reactivity of Ferryl Heme in compounds I and II","volume":"51","author":"Moody","year":"2018","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0620","doi-asserted-by":"crossref","first-page":"5942","DOI":"10.1021\/jacs.9b00795","article-title":"Tuning the geometric and electronic structure of synthetic high-valent Heme Iron(IV)-Oxo models in the presence of a Lewis acid and various axial ligands","volume":"141","author":"Ehudin","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0625","doi-asserted-by":"crossref","first-page":"5756","DOI":"10.1021\/ja00225a028","article-title":"Oxoferryl complexes of the halogenated (porphinato)iron catalyst [tetrakis(2,6-dichlorophenyl)porphinato]iron","volume":"110","author":"Gold","year":"1988","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0630","doi-asserted-by":"crossref","first-page":"3736","DOI":"10.1021\/ja00298a065","article-title":"Formation of an iron(IV)-oxo \"picket-fence\" porphyrin derivative via reduction of the ferrous dioxygen adduct and reaction with carbon dioxide","volume":"107","author":"Schappacher","year":"1985","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0635","doi-asserted-by":"crossref","first-page":"5075","DOI":"10.1021\/ja00484a027","article-title":"The influence of axial ligands on metalloporphyrin visible absorption spectra. Complexes of tetraphenylporphinatozinc","volume":"100","author":"Nappa","year":"1978","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0640","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1038\/ncomms1718","article-title":"The biology and chemistry of high-valent iron\u2013oxo and iron\u2013nitrido complexes","volume":"3","author":"Hohenberger","year":"2012","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0645","doi-asserted-by":"crossref","first-page":"1937","DOI":"10.1126\/science.1128506","article-title":"An octahedral coordination complex of Iron(VI)","volume":"312","author":"Berry","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0650","doi-asserted-by":"crossref","first-page":"5202","DOI":"10.1021\/ic030043r","article-title":"Effect of the sixth axial ligand in CS-ligated Iron(II)octaethylporphyrinates: structural and M\u00f6ssbauer studies","volume":"42","author":"Cao","year":"2003","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0655","doi-asserted-by":"crossref","first-page":"9825","DOI":"10.1021\/ja061618x","article-title":"X-ray absorption spectroscopy and density functional theory studies of [(H3buea)FeIII-X]n\u2013 (X = S2\u2212, O2\u2212, OH\u2212): comparison of bonding and hydrogen bonding in Oxo and Sulfido complexes","volume":"128","author":"Dey","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0660","doi-asserted-by":"crossref","first-page":"12394","DOI":"10.1021\/ja8022576","article-title":"Axial ligand effects on the geometric and electronic structures of Nonheme Oxoiron(IV) complexes","volume":"130","author":"Jackson","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0665","doi-asserted-by":"crossref","first-page":"7819","DOI":"10.1021\/ja00284a054","article-title":"Structural characterization of horseradish peroxidase using EXAFS spectroscopy. Evidence for Fe = O ligation in compounds I and II","volume":"108","author":"Penner-Hahn","year":"1986","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0670","doi-asserted-by":"crossref","first-page":"5707","DOI":"10.1039\/D2SC01232D","article-title":"Heme compound II models in chemoselectivity and disproportionation reactions","volume":"13","author":"Gupta","year":"2022","journal-title":"Chem. Sci."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0675","doi-asserted-by":"crossref","first-page":"8179","DOI":"10.1073\/pnas.0708299105","article-title":"Reactive oxygen species special feature: X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative","volume":"105","author":"Newcomb","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0680","doi-asserted-by":"crossref","first-page":"4361","DOI":"10.1039\/b801803k","article-title":"Electronic structure and spectroscopy of \u201csuperoxidized\u201d iron centers in model systems: theoretical and experimental trends","volume":"10","author":"Berry","year":"2008","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0685","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1002\/chem.200901163","article-title":"Contrasting effects of axial ligands on electron-transfer versus proton-coupled electron-transfer reactions of Nonheme Oxoiron(IV) complexes","volume":"16","author":"Fukuzumi","year":"2010","journal-title":"Chem. Eur. J."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0690","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1021\/ar400258p","article-title":"Tuning reactivity and mechanism in oxidation reactions by mononuclear Nonheme Iron(IV)-Oxo complexes","volume":"47","author":"Nam","year":"2014","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0695","doi-asserted-by":"crossref","DOI":"10.3389\/fphar.2012.00030","article-title":"Direct antioxidant properties of bilirubin and Biliverdin. Is there a role for Biliverdin reductase?","volume":"3","author":"Jansen","year":"2012","journal-title":"Front. Pharmacol."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0700","doi-asserted-by":"crossref","first-page":"10612","DOI":"10.1074\/jbc.M010349200","article-title":"Disruption of an active site hydrogen bond converts human Heme Oxygenase-1 into a peroxidase","volume":"276","author":"Lightning","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0705","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1038\/12319","article-title":"Crystal structure of human heme oxygenase-l","volume":"6","author":"Schuller","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0710","doi-asserted-by":"crossref","first-page":"1758","DOI":"10.1021\/ja962551o","article-title":"Effects of concerted hydrogen bonding of distal histidine on active site structures of horseradish peroxidase. Resonance Raman studies with Asn70 mutants","volume":"119","author":"Mukai","year":"1997","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0715","doi-asserted-by":"crossref","first-page":"14251","DOI":"10.1021\/bi961740g","article-title":"Catalytic roles of the distal site asparagine\u2212histidine couple in peroxidases","volume":"35","author":"Nagano","year":"1996","journal-title":"Biochem."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0720","doi-asserted-by":"crossref","first-page":"12558","DOI":"10.1021\/jacs.9b01253","article-title":"Enhanced rates of C\u2013H Bond cleavage by a Hydrogen-Bonded synthetic Heme High-Valent Iron(IV) Oxo complex","volume":"141","author":"Ehudin","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0725","doi-asserted-by":"crossref","first-page":"8179","DOI":"10.1073\/pnas.0708299105","article-title":"X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative","volume":"105","author":"Newcomb","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0730","doi-asserted-by":"crossref","first-page":"14945","DOI":"10.1039\/C8DT02142B","article-title":"Dramatic rate-enhancement of oxygen atom transfer by an iron(iv)-oxo species by equatorial ligand field perturbations","volume":"47","author":"Mukherjee","year":"2018","journal-title":"Dalton Trans."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0735","doi-asserted-by":"crossref","first-page":"15276","DOI":"10.1021\/jacs.7b06035","article-title":"Tunneling control of chemical reactions: the third reactivity paradigm","volume":"139","author":"Schreiner","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jinorgbio.2023.112367_bb0740","doi-asserted-by":"crossref","first-page":"3618","DOI":"10.1021\/ic403124u","article-title":"Unified view of oxidative C\u2013H Bond cleavage and sulfoxidation by a nonheme Iron(IV)\u2013Oxo complex via lewis acid-promoted electron transfer","volume":"53","author":"Park","year":"2014","journal-title":"Inorg. Chem."}],"container-title":["Journal of Inorganic Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013423002490?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013423002490?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,27]],"date-time":"2025-09-27T15:10:49Z","timestamp":1758985849000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0162013423002490"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,12]]},"references-count":148,"alternative-id":["S0162013423002490"],"URL":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2023.112367","relation":{},"ISSN":["0162-0134"],"issn-type":[{"value":"0162-0134","type":"print"}],"subject":[],"published":{"date-parts":[[2023,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Heme-copper and Heme O2-derived synthetic (bioinorganic) chemistry toward an understanding of cytochrome c oxidase dioxygen chemistry","name":"articletitle","label":"Article Title"},{"value":"Journal of Inorganic Biochemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2023.112367","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"112367"}}