The structure of a ferrous heme-nitro species in the binuclear heme a3/CuB center of ba3-cytochrome c oxidase as determined by resonance Raman spectroscopy
dc.contributor.author | Loullis, Andreas | en |
dc.contributor.author | Noor, M. R. | en |
dc.contributor.author | Soulimane, T. | en |
dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.creator | Loullis, Andreas | en |
dc.creator | Noor, M. R. | en |
dc.creator | Soulimane, T. | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.date.accessioned | 2019-11-21T06:21:16Z | |
dc.date.available | 2019-11-21T06:21:16Z | |
dc.date.issued | 2015 | |
dc.identifier.issn | 1359-7345 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/55811 | |
dc.description.abstract | Members of the cytochrome c oxidase family exhibit nitrite reductase activity. In this work, we have characterized a ferrous heme a3-nitro species in ba3-oxidase by resonance Raman spectroscopy. This provides the first evidence for the structure of a nitrite-bound species in the binuclear heme/copper center of cytochrome c oxidases. © 2015 The Royal Society of Chemistry. | en |
dc.source | Chemical Communications | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84916222383&doi=10.1039%2fc4cc08019j&partnerID=40&md5=0fb0c7a2c2216b4b661b047d1de917dc | |
dc.subject | nonhuman | en |
dc.subject | Article | en |
dc.subject | enzyme activity | en |
dc.subject | chemistry | en |
dc.subject | analogs and derivatives | en |
dc.subject | absorption | en |
dc.subject | chemical structure | en |
dc.subject | oxygen | en |
dc.subject | copper | en |
dc.subject | pH | en |
dc.subject | hydrogen bond | en |
dc.subject | nitrogen | en |
dc.subject | bacterial protein | en |
dc.subject | Bacterial Proteins | en |
dc.subject | cysteine | en |
dc.subject | Models, Molecular | en |
dc.subject | conformational transition | en |
dc.subject | absorption spectroscopy | en |
dc.subject | chemical interaction | en |
dc.subject | Raman spectrometry | en |
dc.subject | heme | en |
dc.subject | myoglobin | en |
dc.subject | Nitrites | en |
dc.subject | Spectrum Analysis, Raman | en |
dc.subject | histidine | en |
dc.subject | Cytochrome b Group | en |
dc.subject | Electron Transport Complex IV | en |
dc.subject | Thermus thermophilus | en |
dc.subject | cytochrome b | en |
dc.subject | cytochrome ba3 | en |
dc.subject | cytochrome c oxidase | en |
dc.subject | heme derivative | en |
dc.subject | nitrite | en |
dc.subject | heme a | en |
dc.subject | nitrite reductase | en |
dc.subject | sodium dithionite | en |
dc.title | The structure of a ferrous heme-nitro species in the binuclear heme a3/CuB center of ba3-cytochrome c oxidase as determined by resonance Raman spectroscopy | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1039/c4cc08019j | |
dc.description.volume | 51 | |
dc.description.issue | 2 | |
dc.description.startingpage | 286 | |
dc.description.endingpage | 289 | |
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 :7</p> | en |
dc.source.abbreviation | Chem.Commun. | en |
dc.contributor.orcid | Pinakoulaki, Eftychia [0000-0003-3320-6112] | |
dc.gnosis.orcid | 0000-0003-3320-6112 |
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