Please use this identifier to cite or link to this item:
Title: The origin of the Fe IV = O intermediates in cytochrome aa 3 oxidase
Authors: Varotsis, Constantinos 
Pinakoulaki, Eftychia 
Daskalakis, Vangelis 
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
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

CORE Recommender
Show full item record

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.