The origin of the Fe IV = O intermediates in cytochrome aa 3 oxidase
dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.contributor.author | Daskalakis, Vangelis | en |
dc.contributor.author | Varotsis, Constantinos | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.creator | Daskalakis, Vangelis | en |
dc.creator | Varotsis, Constantinos | en |
dc.date.accessioned | 2019-11-21T06:22:18Z | |
dc.date.available | 2019-11-21T06:22:18Z | |
dc.date.issued | 2012 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/56025 | |
dc.description.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. © 2011 Elsevier B.V. All rights reserved. | en |
dc.source | Biochimica et Biophysica Acta - Bioenergetics | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84857920643&doi=10.1016%2fj.bbabio.2011.07.009&partnerID=40&md5=620d263e39a5d48cef81ce23ddefe420 | |
dc.subject | article | en |
dc.subject | priority journal | en |
dc.subject | unclassified drug | en |
dc.subject | enzyme activity | en |
dc.subject | Iron | en |
dc.subject | molecular interaction | en |
dc.subject | Ferric Compounds | en |
dc.subject | oxidation reduction reaction | en |
dc.subject | Oxidation-Reduction | en |
dc.subject | oxygen | en |
dc.subject | Biological Transport | en |
dc.subject | copper | en |
dc.subject | catalysis | en |
dc.subject | quantum mechanics | en |
dc.subject | hydrogen bond | en |
dc.subject | electron transport | en |
dc.subject | Molecular Structure | en |
dc.subject | molecular dynamics | en |
dc.subject | Bacterial Proteins | en |
dc.subject | Protein Conformation | en |
dc.subject | proton | en |
dc.subject | proton transport | en |
dc.subject | Binding Sites | en |
dc.subject | Models, Molecular | en |
dc.subject | Models, Chemical | en |
dc.subject | Protons | en |
dc.subject | Raman spectrometry | en |
dc.subject | Resonance Raman spectroscopy | en |
dc.subject | heme | en |
dc.subject | Spectrum Analysis, Raman | en |
dc.subject | vibration | en |
dc.subject | Electron Transport Complex IV | en |
dc.subject | cytochrome c oxidase | en |
dc.subject | oxidoreductase | en |
dc.subject | Heme-copper oxidase | en |
dc.subject | Histidine | en |
dc.subject | Bacillus subtilis | en |
dc.subject | Ferryl intermediate | en |
dc.subject | heme copper oxidoreductase | en |
dc.subject | hydrogen peroxide | en |
dc.subject | Molecular dynamics simulation | en |
dc.subject | propionic acid | en |
dc.title | The origin of the Fe IV = O intermediates in cytochrome aa 3 oxidase | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1016/j.bbabio.2011.07.009 | |
dc.description.volume | 1817 | |
dc.description.issue | 4 | |
dc.description.startingpage | 552 | |
dc.description.endingpage | 557 | |
dc.author.faculty | 002 Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Χημείας / Department of Chemistry | |
dc.type.uhtype | Article | en |
dc.description.notes | <p>Cited By :4</p> | en |
dc.source.abbreviation | Biochim.Biophys.Acta Bioenerg. | en |
dc.contributor.orcid | Pinakoulaki, Eftychia [0000-0003-3320-6112] | |
dc.contributor.orcid | Daskalakis, Vangelis [0000-0001-8870-0850] | |
dc.contributor.orcid | Varotsis, Constantinos [0000-0003-2771-8891] | |
dc.gnosis.orcid | 0000-0003-3320-6112 | |
dc.gnosis.orcid | 0000-0001-8870-0850 | |
dc.gnosis.orcid | 0000-0003-2771-8891 |
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