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|Title:||Nitric oxide activation by caa3 oxidoreductase from Thermus thermophilus||Authors:||Ohta, Takehiro
|Keywords:||Nitric oxide;Thermus thermophilus||Category:||Chemical Sciences||Field:||Natural Sciences||Issue Date:||28-Apr-2015||Publisher:||Royal Society of Chemistry||Source:||Physical Chemistry Chemical Physics, 2015, Volume 17, Issue 16, Pages 10894-10898||metadata.dc.doi:||10.1039/c5cp01013f||Abstract:||Visible and UV-resonance Raman spectroscopy was employed to investigate the reaction of NO with cytochrome caa3 from Thermus thermophilus. We show the formation of the hyponitrite (HO–N[double bond, length as m-dash]N–O)− bound to the heme a3 species (νN[double bond, length as m-dash]N = 1330 cm−1) forming a high spin complex in the oxidized heme a3 Fe/CuB binuclear center of caa3-oxidoreductase. In the absence of heme a3 Fe2+–NO formation, the electron required for the formation of the N[double bond, length as m-dash]N bond originates from the autoreduction of CuB by NO, producing nitrite. With the identification of the hyponitrite intermediate the hypothesis of a common phylogeny of aerobic respiration and bacterial denitrification is fully supported and the mechanism for the 2e−/2H+ reduction of NO to N2O can be described with more certainty.||URI:||http://ktisis.cut.ac.cy/handle/10488/9486||ISSN:||14639076||Rights:||© The Owner Societies 2015.||Type:||Article|
|Appears in Collections:||Άρθρα/Articles|
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