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|Title:||The origin of the Fe IV = O intermediates in cytochrome aa 3 oxidase||Authors:||Varotsis, Constantinos
|Keywords:||Copper;Heme;Hydrogen peroxide;Oxidoreductases;Oxygen;Bacterial Proteins;Biological transport;Protons;Spectrum analysis||Category:||Agriculture,Forestry, and Fisheries||Field:||Agricultural Sciences||Issue Date:||2012||Publisher:||Elsevier||Source:||Biochimica et Biophysica acta - Bioenergetics, 2012, Volume 1817, Issue 4, Pages 552-557||Abstract:||The dioxygen reduction mechanism in cytochrome oxidases relies on proton control of the electron transfer events that drive the process. Proton delivery and proton channels in the protein that are relevant to substrate reduction and proton pumping are considered, and the current status of this area is summarized. We propose a mechanism in which the coupling of the oxygen reduction chemistry to proton translocation (P → F transition) is related to the properties of two groups of highly conserved residues, namely, His411/G386-T389 and the heme a 3-propionateA-D399-H403 chain. This article is part of a Special Issue entitled: Respiratory Oxidases||URI:||http://ktisis.cut.ac.cy/handle/10488/6552||ISSN:||00052728||DOI:||10.1016/j.bbabio.2011.07.009||Collaboration :||Cyprus University of Technology
University of Cyprus
|Rights:||© 2011 Elsevier B.V. All rights reserved||Type:||Article|
|Appears in Collections:||Άρθρα/Articles|
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