Show simple item record

dc.contributor.authorIoannou, Androullaen
dc.contributor.authorLambrou, Alexandraen
dc.contributor.authorDaskalakis, Vangelisen
dc.contributor.authorPinakoulaki, Eftychiaen
dc.creatorIoannou, Androullaen
dc.creatorLambrou, Alexandraen
dc.creatorDaskalakis, Vangelisen
dc.creatorPinakoulaki, Eftychiaen
dc.date.accessioned2019-11-21T06:19:26Z
dc.date.available2019-11-21T06:19:26Z
dc.date.issued2017
dc.identifier.urihttp://gnosis.library.ucy.ac.cy/handle/7/55569
dc.description.abstractThe coordination of nitrite in myoglobin (Mb) has been characterized by resonance Raman spectroscopy and the frequencies of the nitrite bound to the heme Fe as well to the 2-vinyl have been computed by density functional theory (DFT) calculations. The DFT Natural Bond Orbital (NBO) analysis and the extensive isotope-labeling in the resonance Raman experiments indicate that NO2 − (O1[sbnd]N[dbnd]O2) is bound to the heme Fe via O1. Based on the vibrational characterization of the reversible transition between low and high spin Fe[sbnd]O[sbnd]N[dbnd]O/2-nitrovinyl species, we suggest that the key step that triggers the spin-change is the increase of the proximal Fe[sbnd]NHis93 bond length. The frequencies of the O and N sensitive bands of the Fe[sbnd]O[sbnd]N[dbnd]O/2-nitrovinyl species remained largely unchanged in the low- to high-spin transition. Therefore the “greening” process in the reaction of ferric Mb with NO2 − proceeds through the Fe[sbnd]O[sbnd]N[dbnd]O/2-nitrovinyl species, which can exist in either the high or low-spin state. © 2016 Elsevier Inc.en
dc.sourceJournal of inorganic biochemistryen
dc.source.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84995612427&doi=10.1016%2fj.jinorgbio.2016.10.002&partnerID=40&md5=bf9d078f0b9b6f185d47bae883ee6cff
dc.subjectArticleen
dc.subjectAnimalsen
dc.subjectanimalen
dc.subjectchemistryen
dc.subjectRaman spectroscopyen
dc.subjectchemical structureen
dc.subjectferric ionen
dc.subjectdensity functional theoryen
dc.subjectoxygenen
dc.subjectcomplex formationen
dc.subjectnitrogenen
dc.subjectironen
dc.subjectoxidationen
dc.subjecthorseen
dc.subjectHorsesen
dc.subjectRaman spectrometryen
dc.subjecthemeen
dc.subjectHeme proteinsen
dc.subjectmyoglobinen
dc.subjectNitriteen
dc.subjectNitritesen
dc.subjectvinyl derivativeen
dc.subjectDensity functional theory calculationsen
dc.subjectisotope labelingen
dc.titleNitrite coordination in myoglobinen
dc.typeinfo:eu-repo/semantics/article
dc.identifier.doi10.1016/j.jinorgbio.2016.10.002
dc.description.volume166
dc.description.startingpage49
dc.description.endingpage54
dc.author.faculty002 Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences
dc.author.departmentΤμήμα Χημείας / Department of Chemistry
dc.type.uhtypeArticleen
dc.source.abbreviationJ.Inorg.Biochem.en
dc.contributor.orcidPinakoulaki, Eftychia [0000-0003-3320-6112]
dc.contributor.orcidDaskalakis, Vangelis [0000-0001-8870-0850]
dc.gnosis.orcid0000-0003-3320-6112
dc.gnosis.orcid0000-0001-8870-0850


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record