dc.contributor.author | Ioannou, Androulla | en |
dc.contributor.author | Lambrou, Alexandra | en |
dc.contributor.author | Daskalakis, Vangelis | en |
dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.creator | Ioannou, Androulla | en |
dc.creator | Lambrou, Alexandra | en |
dc.creator | Daskalakis, Vangelis | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.date.accessioned | 2019-11-21T06:19:26Z | |
dc.date.available | 2019-11-21T06:19:26Z | |
dc.date.issued | 2017 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/55569 | |
dc.description.abstract | The 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.source | Journal of inorganic biochemistry | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84995612427&doi=10.1016%2fj.jinorgbio.2016.10.002&partnerID=40&md5=bf9d078f0b9b6f185d47bae883ee6cff | |
dc.subject | Article | en |
dc.subject | Animals | en |
dc.subject | animal | en |
dc.subject | chemistry | en |
dc.subject | Raman spectroscopy | en |
dc.subject | chemical structure | en |
dc.subject | ferric ion | en |
dc.subject | density functional theory | en |
dc.subject | oxygen | en |
dc.subject | complex formation | en |
dc.subject | nitrogen | en |
dc.subject | iron | en |
dc.subject | oxidation | en |
dc.subject | horse | en |
dc.subject | Horses | en |
dc.subject | Raman spectrometry | en |
dc.subject | heme | en |
dc.subject | Heme proteins | en |
dc.subject | myoglobin | en |
dc.subject | Nitrite | en |
dc.subject | Nitrites | en |
dc.subject | vinyl derivative | en |
dc.subject | Density functional theory calculations | en |
dc.subject | isotope labeling | en |
dc.title | Nitrite coordination in myoglobin | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1016/j.jinorgbio.2016.10.002 | |
dc.description.volume | 166 | |
dc.description.startingpage | 49 | |
dc.description.endingpage | 54 | |
dc.author.faculty | 002 Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Χημείας / Department of Chemistry | |
dc.type.uhtype | Article | en |
dc.source.abbreviation | J.Inorg.Biochem. | en |
dc.contributor.orcid | Pinakoulaki, Eftychia [0000-0003-3320-6112] | |
dc.contributor.orcid | Daskalakis, Vangelis [0000-0001-8870-0850] | |
dc.gnosis.orcid | 0000-0003-3320-6112 | |
dc.gnosis.orcid | 0000-0001-8870-0850 | |