Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/6550
Title: Regulation of electron and proton transfer by the protein matrix of cytochrome C oxidase
Authors: Farantos, Stavros C. 
Guallar, Victor 
Varotsis, Constantinos 
Daskalakis, Evangelos 
Farantos, Stavros C. 
Keywords: Protons;Lakes;Molecular dynamics;Molecules;Porphyrins;Proteins;Cytochrome oxidase;Heme;Chemistry;Electron Transport
Category: Earth and related Environmental Sciences
Field: Natural Sciences
Issue Date: 2011
Publisher: ACS Publications
Source: Journal of physical chemistry B, 2011, Volume 115, Issue 13, Pages 3648-3655
Abstract: Cytochrome c oxidase (CcO) catalyzes the four-electron reduction of molecular oxygen to water and couples this reduction to the pumping of four protons through the protein matrix. Water molecules inside the protein are involved in the proton pumping activity as proton carriers. A highly conserved water molecule, among different CcO enzymes, lies between the heme a 3 propionates. Here, we show, by quantum mechanical/molecular mechanical (QM/MM) simulations, that this conserved water molecule can transfer its proton to propionate-A. His403 residue coordinates to the Mg site near the so-called water pool. By both QM/MM and molecular dynamics calculations, we demonstrate that the also conserved His403 residue, adjacent to the heme a 3 propionate-A, plays a role of a valve controlling the protonation state of the propionate-A/Asp399 pair. This, in turn, controls the oxidation state of the heme a 3 iron, linking in this way, the D-proton pathway to the water pool
URI: http://ktisis.cut.ac.cy/handle/10488/6550
ISSN: 15206106
DOI: 10.1021/jp1115993
Rights: © 2011 American Chemical Society
Type: Article
Appears in Collections:Άρθρα/Articles

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