Please use this identifier to cite or link to this item:
|Title:||Nitrite coordination in myoglobin||Authors:||Ioannou, Androulla
|Keywords:||Density functional theory calculations;Heme proteins;Nitrite;Raman spectroscopy||Category:||Chemical Sciences||Field:||Natural Sciences||Issue Date:||1-Jan-2017||Publisher:||Elsevier Inc.||Source:||Journal of Inorganic Biochemistry,1 January 2017,Volume 166, Pages 49-54||metadata.dc.doi:||http://dx.doi.org/10.1016/j.jinorgbio.2016.10.002||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.||URI:||http://ktisis.cut.ac.cy/handle/10488/9345||ISSN:||01620134||Rights:||© 2016 Elsevier Inc.||Type:||Article|
|Appears in Collections:||Άρθρα/Articles|
Show full item record
Page view(s) 1052
checked on Dec 18, 2017
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.