dc.contributor.author | Koutsoupakis, Constantinos | en |
dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.contributor.author | Stavrakis, Stavros | en |
dc.contributor.author | Daskalakis, Vangelis | en |
dc.contributor.author | Varotsis, Constantinos | en |
dc.creator | Koutsoupakis, Constantinos | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.creator | Stavrakis, Stavros | en |
dc.creator | Daskalakis, Vangelis | en |
dc.creator | Varotsis, Constantinos | en |
dc.date.accessioned | 2019-11-21T06:20:56Z | |
dc.date.available | 2019-11-21T06:20:56Z | |
dc.date.issued | 2004 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/55740 | |
dc.description.abstract | We have applied FTIR and time-resolved step-scan Fourier transform infrared (TRS2-FTIR) spectroscopy to investigate the dynamics of the heme-CuB binuclear center and the protein dynamics of mammalian aa3, Pseudomonas stutzeri cbb3, and caa3 and ba3 from Thermus thermophilus cytochrome oxidases. The implications of these results with respect to (1) the molecular motions that are general to the photodynamics of the binuclear center in heme-copper oxidases, and (2) the proton pathways located in the ring A propionate of heme a3-Asp372- H2O site that is conserved among all structurally known oxidases are discussed. © 2004 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-s2.0-1942504432&doi=10.1016%2fj.bbabio.2003.06.004&partnerID=40&md5=25d0caec75e7c7704d827a18b356981e | |
dc.subject | priority journal | en |
dc.subject | review | en |
dc.subject | nonhuman | en |
dc.subject | Animals | en |
dc.subject | enzyme activity | en |
dc.subject | molecular interaction | en |
dc.subject | oxygen | en |
dc.subject | analytic method | en |
dc.subject | infrared spectroscopy | en |
dc.subject | water | en |
dc.subject | Cattle | en |
dc.subject | FTIR | en |
dc.subject | molecular dynamics | en |
dc.subject | Pseudomonas | en |
dc.subject | Mammalia | en |
dc.subject | Models, Molecular | en |
dc.subject | Spectroscopy, Fourier Transform Infrared | en |
dc.subject | Resonance Raman | en |
dc.subject | CcO | en |
dc.subject | Cytochrome b Group | en |
dc.subject | Cytochrome c Group | en |
dc.subject | Cytochrome c oxidase | en |
dc.subject | Cytochromes a | en |
dc.subject | Cytochromes a3 | en |
dc.subject | Electron Transport Complex IV | en |
dc.subject | Fourier transform infrared | en |
dc.subject | heme oxygenase | en |
dc.subject | MCT | en |
dc.subject | Mercury cadmium telluride | en |
dc.subject | photodegradation | en |
dc.subject | Proton-Motive Force | en |
dc.subject | Pseudomonas stutzeri | en |
dc.subject | RR | en |
dc.subject | structural homology | en |
dc.subject | Thermus | en |
dc.subject | Thermus thermophilus | en |
dc.subject | Time-resolved Fourier transform infrared | en |
dc.subject | TR-FTIR | en |
dc.title | Time-resolved step-scan Fourier transform infrared investigation of heme-copper oxidases: Implications for O2 input and H 2O/H+ output channels | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1016/j.bbabio.2003.06.004 | |
dc.description.volume | 1655 | |
dc.description.issue | 1-3 | |
dc.description.startingpage | 347 | |
dc.description.endingpage | 352 | |
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 :21</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 | |