dc.contributor.author | Lambrou, Alexandra | en |
dc.contributor.author | Ioannou, Androulla | en |
dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.creator | Lambrou, Alexandra | en |
dc.creator | Ioannou, Androulla | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.date.accessioned | 2019-11-21T06:21:01Z | |
dc.date.available | 2019-11-21T06:21:01Z | |
dc.date.issued | 2016 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/55756 | |
dc.description.abstract | The myoglobin (Mb) heme Fe-O-N=O and heme Fe-O-N=O/2-nitrovinyl species have been characterized by resonance Raman spectroscopy. In the heme Fe-O-N=O species, the bound nitrite ligand is removed by solvent exchange, thus reforming metmyoglobin (metMb). The high-spin heme Fe-O-N=O unit is converted into a low-spin heme Fe-O-N=O/2-nitrovinyl species that can be reversibly switched between a low- and a high-spin state without removing the bound nitrite ligand, as observed in the case of the heme Fe-O-N=O species. This spin-state change is likely to be accompanied by a general structural rearrangement in the protein-binding pocket. This example is the first of a globin protein that can reversibly change its metal spin state through an internal perturbation. These findings provide a basis for understanding the structure–function relationship of the spin cross found in other metalloenzymes and FeIII–porphyrin complexes. © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim | en |
dc.source | Chemistry - A European Journal | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84981205626&doi=10.1002%2fchem.201601738&partnerID=40&md5=8c4d7ce720d2946284565aae45622d7a | |
dc.subject | Spin dynamics | en |
dc.subject | Raman spectroscopy | en |
dc.subject | Iron compounds | en |
dc.subject | Ligands | en |
dc.subject | Drug products | en |
dc.subject | Biochemistry | en |
dc.subject | Proteins | en |
dc.subject | Resonance Raman spectroscopy | en |
dc.subject | Function relationships | en |
dc.subject | heme proteins | en |
dc.subject | Internal perturbation | en |
dc.subject | nitrite ligands | en |
dc.subject | Porphyrin complexes | en |
dc.subject | Porphyrins | en |
dc.subject | spin crossover | en |
dc.subject | Spin crossovers | en |
dc.subject | Spin-state changes | en |
dc.subject | Structural rearrangement | en |
dc.title | Spin Crossover in Nitrito-Myoglobin as Revealed by Resonance Raman Spectroscopy | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1002/chem.201601738 | |
dc.description.volume | 22 | |
dc.description.issue | 34 | |
dc.description.startingpage | 12176 | |
dc.description.endingpage | 12180 | |
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.description.notes | <p>Cited By :2</p> | en |
dc.source.abbreviation | Chem.Eur.J. | en |
dc.contributor.orcid | Pinakoulaki, Eftychia [0000-0003-3320-6112] | |
dc.gnosis.orcid | 0000-0003-3320-6112 | |