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https://hdl.handle.net/20.500.14279/3191
Πεδίο DC | Τιμή | Γλώσσα |
---|---|---|
dc.contributor.author | Varotsis, Constantinos | - |
dc.contributor.author | Pinakoulaki, Eftychia | - |
dc.contributor.author | Daskalakis, Vangelis | - |
dc.date.accessioned | 2013-01-16T13:45:50Z | en |
dc.date.accessioned | 2013-05-17T07:13:15Z | - |
dc.date.accessioned | 2015-12-02T14:27:34Z | - |
dc.date.available | 2013-01-16T13:45:50Z | en |
dc.date.available | 2013-05-17T07:13:15Z | - |
dc.date.available | 2015-12-02T14:27:34Z | - |
dc.date.issued | 2012-04 | - |
dc.identifier.citation | Biochimica et Biophysica acta - Bioenergetics, 2012, vol.1817, no.4, pp. 552-557 | en_US |
dc.identifier.issn | 00052728 | - |
dc.identifier.uri | https://hdl.handle.net/20.500.14279/3191 | - |
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 | en_US |
dc.format | en_US | |
dc.language.iso | en | en_US |
dc.relation.ispartof | Biochimica et Biophysica Acta - Bioenergetics | en_US |
dc.rights | © 2011 Elsevier | en_US |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 United States | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/us/ | * |
dc.subject | Copper | en_US |
dc.subject | Heme | en_US |
dc.subject | Hydrogen peroxide | en_US |
dc.subject | Oxidoreductases | en_US |
dc.subject | Oxygen | en_US |
dc.subject | Bacterial Proteins | en_US |
dc.subject | Biological transport | en_US |
dc.subject | Protons | en_US |
dc.subject | Spectrum analysis | en_US |
dc.title | The origin of the FeIV = O intermediates in cytochrome aa3 oxidase | en_US |
dc.type | Article | en_US |
dc.collaboration | Cyprus University of Technology | en_US |
dc.collaboration | University of Cyprus | en_US |
dc.journals | Open Access | en_US |
dc.review | peer reviewed | - |
dc.country | Cyprus | en_US |
dc.subject.field | Agricultural Sciences | en_US |
dc.identifier.doi | 10.1016/j.bbabio.2011.07.009 | en_US |
dc.dept.handle | 123456789/70 | en |
dc.relation.issue | 4 | en_US |
dc.relation.volume | 1817 | en_US |
cut.common.academicyear | 2011-2012 | en_US |
dc.identifier.spage | 552 | en_US |
dc.identifier.epage | 557 | en_US |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
item.grantfulltext | none | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.cerifentitytype | Publications | - |
item.openairetype | article | - |
crisitem.journal.journalissn | 0005-2728 | - |
crisitem.journal.publisher | Elsevier | - |
crisitem.author.dept | Department of Chemical Engineering | - |
crisitem.author.dept | Department of Chemical Engineering | - |
crisitem.author.faculty | Faculty of Geotechnical Sciences and Environmental Management | - |
crisitem.author.faculty | Faculty of Geotechnical Sciences and Environmental Management | - |
crisitem.author.orcid | 0000-0003-2771-8891 | - |
crisitem.author.orcid | 0000-0001-8870-0850 | - |
crisitem.author.parentorg | Faculty of Geotechnical Sciences and Environmental Management | - |
crisitem.author.parentorg | Faculty of Geotechnical Sciences and Environmental Management | - |
Εμφανίζεται στις συλλογές: | Άρθρα/Articles |
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