dc.contributor.author | Stavrakis, Stavros | en |
dc.contributor.author | Koutsoupakis, Constantinos | en |
dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.contributor.author | Urban, A. | en |
dc.contributor.author | Saraste, M. | en |
dc.contributor.author | Varotsis, Constantinos | en |
dc.creator | Stavrakis, Stavros | en |
dc.creator | Koutsoupakis, Constantinos | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.creator | Urban, A. | en |
dc.creator | Saraste, M. | en |
dc.creator | Varotsis, Constantinos | en |
dc.date.accessioned | 2019-11-21T06:22:56Z | |
dc.date.available | 2019-11-21T06:22:56Z | |
dc.date.issued | 2002 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/56152 | |
dc.description.abstract | Time-resolved step-scan Fourier infrared spectroscopy has been used to study the CO-bound cbb3-type cytochrome c oxidase from Pseudomonas stutzeri at room temperature. We observe a single band in the FTIR spectrum at 1956 cm-1 (β-form). The time-resolved data indicate that upon photolysis, CO is transferred from heme b3 (vCO = 1956 cm-1) to CuB (vCO = 2064 cm-1). The decay of the 2065 cm-1 peak (t1/2 = 120 ± 16 ms) and the development of the 1956 cm-1 peak (t1/2 = 144 ± 8 ms ) suggest that formation of the Fe-CO complex is concurrent with the decay of the CuB-CO complex. The intensity ratio of the Fe-CO/CuB-CO (2.15) remains constant for all data points, and thus we conclude that no fraction of CO escapes the binuclear center at 293 K. Copyright © 2002 American Chemical Society. | en |
dc.source | Journal of the American Chemical Society | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037123251&doi=10.1021%2fja0169825&partnerID=40&md5=5a8eab17f7889e55d269cad947056f1a | |
dc.subject | article | en |
dc.subject | unclassified drug | en |
dc.subject | nonhuman | en |
dc.subject | chemical analysis | en |
dc.subject | Iron | en |
dc.subject | molecular interaction | en |
dc.subject | structure analysis | en |
dc.subject | complex formation | en |
dc.subject | infrared spectroscopy | en |
dc.subject | environmental temperature | en |
dc.subject | Spectroscopy, Fourier Transform Infrared | en |
dc.subject | Raman spectrometry | en |
dc.subject | carbon monoxide | en |
dc.subject | Electron Transport Complex IV | en |
dc.subject | Pseudomonas stutzeri | en |
dc.subject | copper complex | en |
dc.subject | heme derivative | en |
dc.subject | Heme | en |
dc.subject | cytochrome | en |
dc.subject | cytochrome cbb 3 | en |
dc.subject | iron derivative | en |
dc.title | Decay of the transient CuB-CO complex is accompanied by formation of the heme Fe-CO complex of cytochrome cbb3-CO at ambient temperature: Evidence from time-resolved fourier transform infrared spectroscopy | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1021/ja0169825 | |
dc.description.volume | 124 | |
dc.description.issue | 15 | |
dc.description.startingpage | 3814 | |
dc.description.endingpage | 3815 | |
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 :50</p> | en |
dc.source.abbreviation | J.Am.Chem.Soc. | en |
dc.contributor.orcid | Pinakoulaki, Eftychia [0000-0003-3320-6112] | |
dc.contributor.orcid | Varotsis, Constantinos [0000-0003-2771-8891] | |
dc.gnosis.orcid | 0000-0003-3320-6112 | |
dc.gnosis.orcid | 0000-0003-2771-8891 | |