Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/9345
Title: Nitrite coordination in myoglobin
Authors: Ioannou, Androulla 
Lambrou, Alexandra 
Daskalakis, Evangelos 
Pinakoulaki, Eftychia 
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
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