| 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/7/55757 | |
| dc.source.uri | https://nls.ldls.org.uk/welcome.html?ark:/81055/vdc_100035112509.0x00002b | |
| dc.subject | Chemistry | en |
| dc.title | Spin Crossover in Nitrito‐Myoglobin as Revealed by Resonance Raman Spectroscopy | en |
| dc.type | info:eu-repo/semantics/article | |
| 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>ID: 1124 | en |
| dc.description.notes | In: Chemistry, Vol. 22, no. 34 ( 2016), p.12176-12180. | en |
| dc.description.notes | Summary: AbstractThe 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.AbstractSwitching over: The heme Fe‐O‐N=O/ 2‐nitrovinyl myoglobin species can be reversibly switched between low‐ and high‐spin states (see figure | en |
| dc.description.notes | NMb=nitri‐myoglobin). 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.</p> | en |
| dc.contributor.orcid | Pinakoulaki, Eftychia [0000-0003-3320-6112] | |
| dc.gnosis.orcid | 0000-0003-3320-6112 | |
