{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T04:24:28Z","timestamp":1768451068514,"version":"3.49.0"},"reference-count":52,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,6,9]],"date-time":"2023-06-09T00:00:00Z","timestamp":1686268800000},"content-version":"am","delay-in-days":312,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100016251","name":"Hemophilia Center of Western Pennsylvania","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100016251","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P01 HL103455"],"award-info":[{"award-number":["P01 HL103455"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 HL125886"],"award-info":[{"award-number":["R01 HL125886"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["T32 HL110849"],"award-info":[{"award-number":["T32 HL110849"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007921","name":"University of Pittsburgh","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007921","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Nitric Oxide"],"published-print":{"date-parts":[[2022,8]]},"DOI":"10.1016\/j.niox.2022.06.001","type":"journal-article","created":{"date-parts":[[2022,6,3]],"date-time":"2022-06-03T20:56:41Z","timestamp":1654289801000},"page":"12-22","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"special_numbering":"C","title":["Regulation of nitrite reductase and lipid binding properties of cytoglobin by surface and distal histidine mutations"],"prefix":"10.1016","volume":"125-126","author":[{"given":"Stefan J.","family":"Kaliszuk","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Natasha I.","family":"Morgan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Taylor N.","family":"Ayers","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Courtney E.","family":"Sparacino-Watkins","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anthony W.","family":"DeMartino","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kaitlin","family":"Bocian","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Venkata","family":"Ragireddy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qin","family":"Tong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jes\u00fas","family":"Tejero","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"27","key":"10.1016\/j.niox.2022.06.001_bib1","doi-asserted-by":"crossref","first-page":"25318","DOI":"10.1074\/jbc.M102630200","article-title":"Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells","volume":"276","author":"Kawada","year":"2001","journal-title":"J. Biol. Chem."},{"issue":"22","key":"10.1016\/j.niox.2022.06.001_bib2","doi-asserted-by":"crossref","first-page":"19538","DOI":"10.1074\/jbc.M201934200","article-title":"A ubiquitously expressed human hexacoordinate hemoglobin","volume":"277","author":"Trent","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.niox.2022.06.001_bib3","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1093\/oxfordjournals.molbev.a004096","article-title":"Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues","volume":"19","author":"Burmester","year":"2002","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.niox.2022.06.001_bib4","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2020.101468","article-title":"Emerging perspectives on cytoglobin, beyond NO dioxygenase and peroxidase","volume":"32","author":"Mathai","year":"2020","journal-title":"Redox Biol."},{"key":"10.1016\/j.niox.2022.06.001_bib5","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2020.101687","article-title":"Lessons from the post-genomic era: globin diversity beyond oxygen binding and transport","volume":"37","author":"Keppner","year":"2020","journal-title":"Redox Biol."},{"issue":"3","key":"10.1016\/j.niox.2022.06.001_bib6","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1111\/apha.12312","article-title":"Function and evolution of vertebrate globins","volume":"211","author":"Burmester","year":"2014","journal-title":"Acta Physiol."},{"issue":"11","key":"10.1016\/j.niox.2022.06.001_bib7","doi-asserted-by":"crossref","first-page":"3553","DOI":"10.1093\/molbev\/mss164","article-title":"Widespread occurrence of N-terminal acylation in animal globins and possible origin of respiratory globins from a membrane-bound ancestor","volume":"29","author":"Blank","year":"2012","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.niox.2022.06.001_bib8","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.niox.2015.12.004","article-title":"Characterization of zebrafish neuroglobin and cytoglobins 1 and 2: zebrafish cytoglobins provide insights into the transition from six-coordinate to five-coordinate globins","volume":"53","author":"Corti","year":"2016","journal-title":"Nitric Oxide"},{"key":"10.1016\/j.niox.2022.06.001_bib9","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.jinorgbio.2017.04.025","article-title":"Antarctic fish versus human cytoglobins - the same but yet so different","volume":"173","author":"Cuypers","year":"2017","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.niox.2022.06.001_bib10","doi-asserted-by":"crossref","first-page":"2132","DOI":"10.1016\/j.csbj.2020.08.007","article-title":"Structural and functional properties of Antarctic fish cytoglobins-1: cold-reactivity in multi-ligand reactions","volume":"18","author":"Giordano","year":"2020","journal-title":"Comput. Struct. Biotechnol. J."},{"issue":"3","key":"10.1016\/j.niox.2022.06.001_bib11","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1042\/BJ20101136","article-title":"Lipid binding to cytoglobin leads to a change in haem co-ordination: a role for cytoglobin in lipid signalling of oxidative stress","volume":"434","author":"Reeder","year":"2011","journal-title":"Biochem. J."},{"issue":"5","key":"10.1016\/j.niox.2022.06.001_bib12","first-page":"391","article-title":"Peroxidase activation of cytoglobin by anionic phospholipids: mechanisms and consequences","volume":"1861","author":"Tejero","year":"2016","journal-title":"BBA-Mol. Cell Biol. L."},{"issue":"1","key":"10.1016\/j.niox.2022.06.001_bib13","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1042\/BJ20140827","article-title":"Cytoglobin ligand binding regulated by changing haem-co-ordination in response to intramolecular disulfide bond formation and lipid interaction","volume":"465","author":"Beckerson","year":"2015","journal-title":"Biochem. J."},{"issue":"11","key":"10.1016\/j.niox.2022.06.001_bib14","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1016\/j.freeradbiomed.2009.03.004","article-title":"Cytochrome c\/cardiolipin relations in mitochondria: a kiss of death","volume":"46","author":"Kagan","year":"2009","journal-title":"Free Radic. Biol. Med."},{"issue":"15","key":"10.1016\/j.niox.2022.06.001_bib15","doi-asserted-by":"crossref","first-page":"3621","DOI":"10.1111\/febs.12352","article-title":"Differences in oxygen-dependent nitric oxide metabolism by cytoglobin and myoglobin account for their differing functional roles","volume":"280","author":"Liu","year":"2013","journal-title":"FEBS J."},{"issue":"29","key":"10.1016\/j.niox.2022.06.001_bib16","doi-asserted-by":"crossref","first-page":"3212","DOI":"10.1021\/acs.biochem.9b00406","article-title":"The zebrafish cytochrome b5\/cytochrome b5 reductase\/NADH system efficiently reduces cytoglobins 1 and 2: conserved activity of cytochrome b5\/cytochrome b5 reductases during vertebrate evolution","volume":"58","author":"Amdahl","year":"2019","journal-title":"Biochemistry"},{"key":"10.1016\/j.niox.2022.06.001_bib17","doi-asserted-by":"crossref","first-page":"3993","DOI":"10.1021\/acs.biochem.7b00224","article-title":"Efficient reduction of vertebrate cytoglobins by the cytochrome b5\/cytochrome b5 reductase\/NADH system","volume":"56","author":"Amdahl","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.niox.2022.06.001_bib18","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.RA120.016394","article-title":"Defining the reducing system of the NO dioxygenase cytoglobin in vascular smooth muscle cells and its critical role in regulating cellular NO decay","volume":"296","author":"Ilangovan","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.niox.2022.06.001_bib19","article-title":"Cytoglobin regulates blood pressure and vascular tone through nitric oxide metabolism in the vascular wall","volume":"8","author":"Liu","year":"2017","journal-title":"Nat. Commun."},{"issue":"43","key":"10.1016\/j.niox.2022.06.001_bib20","doi-asserted-by":"crossref","first-page":"36623","DOI":"10.1074\/jbc.M112.342378","article-title":"Characterization of the mechanism and magnitude of cytoglobin-mediated nitrite reduction and nitric oxide generation under anaerobic conditions","volume":"287","author":"Li","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.niox.2022.06.001_bib21","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.niox.2017.11.004","article-title":"Strong modulation of nitrite reductase activity of cytoglobin by disulfide bond oxidation: implications for nitric oxide homeostasis","volume":"72","author":"Reeder","year":"2018","journal-title":"Nitric Oxide"},{"issue":"21","key":"10.1016\/j.niox.2022.06.001_bib22","doi-asserted-by":"crossref","first-page":"15918","DOI":"10.1021\/acs.inorgchem.1c01048","article-title":"Endogenous hemoprotein-dependent signaling pathways of nitric oxide and nitrite","volume":"60","author":"Dent","year":"2021","journal-title":"Inorg. Chem."},{"issue":"52","key":"10.1016\/j.niox.2022.06.001_bib23","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2105053118","article-title":"Cytoglobin has potent superoxide dismutase function","volume":"118","author":"Zweier","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.niox.2022.06.001_bib24","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/j.freeradbiomed.2020.10.321","article-title":"Redox sensor properties of human cytoglobin allosterically regulate heme pocket reactivity","volume":"162","author":"DeMartino","year":"2021","journal-title":"Free Radic. Biol. Med."},{"issue":"3","key":"10.1016\/j.niox.2022.06.001_bib25","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1021\/bi501196k","article-title":"Exploring the mechanisms of the reductase activity of neuroglobin by site-directed mutagenesis of the heme distal pocket","volume":"54","author":"Tejero","year":"2015","journal-title":"Biochemistry"},{"issue":"20","key":"10.1016\/j.niox.2022.06.001_bib26","doi-asserted-by":"crossref","first-page":"18277","DOI":"10.1074\/jbc.M110.159541","article-title":"Human neuroglobin functions as a redox-regulated nitrite reductase","volume":"286","author":"Tiso","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.niox.2022.06.001_bib27","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/j.bbrc.2019.12.089","article-title":"Negative surface charges in neuroglobin modulate the interaction with cytochrome c","volume":"523","author":"Tejero","year":"2020","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"5","key":"10.1016\/j.niox.2022.06.001_bib28","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1021\/bi00300a009","article-title":"Influence of the R----T transition on the optical absorption and magnetic circular dichroism spectra of methemoglobin fluoride, aquomethemoglobin, and hydroxymethemoglobin","volume":"23","author":"Rots","year":"1984","journal-title":"Biochemistry"},{"key":"10.1016\/j.niox.2022.06.001_bib29","doi-asserted-by":"crossref","first-page":"87","DOI":"10.12688\/f1000research.5971.1","article-title":"Effect of the distal histidine on the peroxidatic activity of monomeric cytoglobin","volume":"4","author":"Beckerson","year":"2015","journal-title":"F1000Research"},{"issue":"42","key":"10.1016\/j.niox.2022.06.001_bib30","doi-asserted-by":"crossref","first-page":"38949","DOI":"10.1074\/jbc.M106438200","article-title":"Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family","volume":"276","author":"Dewilde","year":"2001","journal-title":"J. Biol. Chem."},{"issue":"51","key":"10.1016\/j.niox.2022.06.001_bib31","doi-asserted-by":"crossref","first-page":"51713","DOI":"10.1074\/jbc.M309396200","article-title":"The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin","volume":"278","author":"Hamdane","year":"2003","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.niox.2022.06.001_bib32","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/nrd2466","article-title":"The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics","volume":"7","author":"Lundberg","year":"2008","journal-title":"Nat. Rev. Drug Discov."},{"issue":"6","key":"10.1016\/j.niox.2022.06.001_bib33","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1038\/nchembio1105-308","article-title":"The emerging biology of the nitrite anion","volume":"1","author":"Gladwin","year":"2005","journal-title":"Nat. Chem. Biol."},{"issue":"1","key":"10.1016\/j.niox.2022.06.001_bib34","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1152\/physrev.00036.2017","article-title":"Sources of vascular nitric oxide and reactive oxygen species and their regulation","volume":"99","author":"Tejero","year":"2019","journal-title":"Physiol. Rev."},{"issue":"8","key":"10.1016\/j.niox.2022.06.001_bib35","doi-asserted-by":"crossref","first-page":"2099","DOI":"10.1172\/JCI24650","article-title":"Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control","volume":"115","author":"Huang","year":"2005","journal-title":"J. Clin. Invest."},{"issue":"12","key":"10.1016\/j.niox.2022.06.001_bib36","doi-asserted-by":"crossref","first-page":"1498","DOI":"10.1038\/nm954","article-title":"Nitrite reduction to nitric oxide by deoxyhemoglobin vasodilates the human circulation","volume":"9","author":"Cosby","year":"2003","journal-title":"Nat. Med."},{"issue":"5","key":"10.1016\/j.niox.2022.06.001_bib37","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1161\/01.RES.0000260171.52224.6b","article-title":"Deoxymyoglobin is a nitrite reductase that generates nitric oxide and regulates mitochondrial respiration","volume":"100","author":"Shiva","year":"2007","journal-title":"Circ. Res."},{"issue":"25","key":"10.1016\/j.niox.2022.06.001_bib38","doi-asserted-by":"crossref","first-page":"5072","DOI":"10.1021\/bi300291h","article-title":"Characterization of the function of cytoglobin as an oxygen-dependent regulator of nitric oxide concentration","volume":"51","author":"Liu","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.niox.2022.06.001_bib39","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.niox.2016.04.007","article-title":"Regulating the nitrite reductase activity of myoglobin by redesigning the heme active center","volume":"57","author":"Wu","year":"2016","journal-title":"Nitric Oxide"},{"issue":"36","key":"10.1016\/j.niox.2022.06.001_bib40","doi-asserted-by":"crossref","first-page":"12452","DOI":"10.1021\/bi980516j","article-title":"Imidazole is a sensitive probe of steric hindrance in the distal pockets of oxygen-binding heme proteins","volume":"37","author":"Mansy","year":"1998","journal-title":"Biochemistry"},{"issue":"50","key":"10.1016\/j.niox.2022.06.001_bib41","doi-asserted-by":"crossref","first-page":"18119","DOI":"10.1021\/ja904726q","article-title":"The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron","volume":"131","author":"Yi","year":"2009","journal-title":"J. Am. Chem. Soc."},{"issue":"32","key":"10.1016\/j.niox.2022.06.001_bib42","doi-asserted-by":"crossref","first-page":"4788","DOI":"10.1021\/acs.biochem.8b00542","article-title":"Nitrosyl myoglobins and their nitrite precursors: crystal structural and quantum mechanics and molecular mechanics theoretical investigations of preferred Fe -no ligand orientations in myoglobin distal pockets","volume":"57","author":"Wang","year":"2018","journal-title":"Biochemistry"},{"issue":"8","key":"10.1016\/j.niox.2022.06.001_bib43","doi-asserted-by":"crossref","first-page":"3059","DOI":"10.1021\/ja512941j","article-title":"Resolution of key roles for the distal pocket histidine in cytochrome C nitrite reductases","volume":"137","author":"Lockwood","year":"2015","journal-title":"J. Am. Chem. Soc."},{"issue":"4","key":"10.1016\/j.niox.2022.06.001_bib44","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1042\/BCJ20200596","article-title":"Influence of the heme distal pocket on nitrite binding orientation and reactivity in Sperm Whale myoglobin","volume":"478","author":"Tse","year":"2021","journal-title":"Biochem. J."},{"issue":"33","key":"10.1016\/j.niox.2022.06.001_bib45","doi-asserted-by":"crossref","first-page":"9406","DOI":"10.1021\/bi7007068","article-title":"Structure and ligand binding properties of myoglobins reconstituted with monodepropionated heme: functional role of each heme propionate side chain","volume":"46","author":"Harada","year":"2007","journal-title":"Biochemistry"},{"issue":"19","key":"10.1016\/j.niox.2022.06.001_bib46","doi-asserted-by":"crossref","first-page":"4697","DOI":"10.1021\/bi00233a009","article-title":"Contributions of residue 45(CD3) and heme-6-propionate to the biomolecular and geminate recombination reactions of myoglobin","volume":"30","author":"Carver","year":"1991","journal-title":"Biochemistry"},{"issue":"4","key":"10.1016\/j.niox.2022.06.001_bib47","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1016\/j.bbrc.2012.07.032","article-title":"Tyrosine B10 triggers a heme propionate hydrogen bonding network loop with glutamine E7 moiety","volume":"424","author":"Ramos-Santana","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"4","key":"10.1016\/j.niox.2022.06.001_bib48","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1021\/ja807420k","article-title":"A role of the heme-7-propionate side chain in cytochrome P450cam as a gate for regulating the access of water molecules to the substrate-binding site","volume":"131","author":"Hayashi","year":"2009","journal-title":"J. Am. Chem. Soc."},{"issue":"4","key":"10.1016\/j.niox.2022.06.001_bib49","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/j.jmb.2004.04.024","article-title":"Structural basis of human cytoglobin for ligand binding","volume":"339","author":"Sugimoto","year":"2004","journal-title":"J. Mol. Biol."},{"issue":"1","key":"10.1016\/j.niox.2022.06.001_bib50","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0049770","article-title":"CO rebinding kinetics and molecular dynamics simulations highlight dynamic regulation of internal cavities in human cytoglobin","volume":"8","author":"Gabba","year":"2013","journal-title":"PLoS One"},{"issue":"31","key":"10.1016\/j.niox.2022.06.001_bib51","doi-asserted-by":"crossref","first-page":"23850","DOI":"10.1074\/jbc.M110.132340","article-title":"Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes","volume":"285","author":"Gardner","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.niox.2022.06.001_bib52","series-title":"The PyMOL Molecular Graphics System","author":"DeLano","year":"2002"}],"container-title":["Nitric Oxide"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1089860322000568?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1089860322000568?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T18:07:42Z","timestamp":1761070062000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1089860322000568"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,8]]},"references-count":52,"alternative-id":["S1089860322000568"],"URL":"https:\/\/doi.org\/10.1016\/j.niox.2022.06.001","relation":{},"ISSN":["1089-8603"],"issn-type":[{"value":"1089-8603","type":"print"}],"subject":[],"published":{"date-parts":[[2022,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Regulation of nitrite reductase and lipid binding properties of cytoglobin by surface and distal histidine mutations","name":"articletitle","label":"Article Title"},{"value":"Nitric Oxide","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.niox.2022.06.001","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}