Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/9411
Title: Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature
Authors: Daskalakis, Evangelos 
Ohta, Takehiro 
Kitagawa, Teizo 
Varotsis, Constantinos 
Keywords: Density functional theory;Heme proteins;Hyponitrite;Oxidoreductases;UV Raman spectroscopy
Category: Biological Sciences
Field: Natural Sciences
Issue Date: 14-Jul-2015
Publisher: Elsevier
Source: Biochimica et Biophysica Acta - Bioenergetics, 2015, Volume 1847, Issue 10, Article number 47495, Pages 1240-1244
metadata.dc.doi: http://dx.doi.org/10.1016/j.bbabio.2015.06.014
Abstract: Nitric oxide reductase (Nor) is the third of the four enzymes of bacterial denitrification responsible for the catalytic formation of laughing gas (N2O). Here we report the detection of the hyponitrite (HO-N = N-O-) species (νN-N = 1332 cm- 1) in the heme b3 Fe-FeB dinuclear center of Nor from Paracoccus denitrificans. We have also applied density functional theory (DFT) to characterize the bimetallic-bridging hyponitrite species in the reduction of NO to N2O by Nor and compare the present results with those recently reported for the N-N bond formation in the ba3 and caa3 oxidoreductases from Thermus thermophilus.
URI: http://ktisis.cut.ac.cy/handle/10488/9411
ISSN: 00052728
Rights: © 2015 Published by Elsevier B.V.
Type: Article
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