Detection of a photostable five-coordinate heme a3-Fe-Co species and functional implications of His384/α10 in CO-bound ba 3-cytochrome c oxidase from Thermus thermophilus
dc.contributor.author | Ohta, T. | en |
dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.contributor.author | Soulimane, T. | en |
dc.contributor.author | Kitagawa, T. | en |
dc.contributor.author | Varotsis, Constantinos | en |
dc.creator | Ohta, T. | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.creator | Soulimane, T. | en |
dc.creator | Kitagawa, T. | en |
dc.creator | Varotsis, Constantinos | en |
dc.date.accessioned | 2019-11-21T06:21:47Z | |
dc.date.available | 2019-11-21T06:21:47Z | |
dc.date.issued | 2004 | |
dc.identifier.issn | 1520-6106 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/55917 | |
dc.description.abstract | Resonance Raman (RR) spectra are reported for the fully reduced carbon monoxy derivative of ba3-cytochrome c oxidase from Thermus thermophilus. The RR spectra show the formation of a photolabile six-coordinate heme-CO and a photostable five-coordinate heme Fe-CO species. The latter species is formed by the cleavage of the proximal heme Fe-His384 bond and is the first five-coordinate Fe-CO species detected in heme-copper oxidases. The frequency of the Fe-CO species observed at 526 cm-1 correlates with either the C-O stretching modes observed at 1967 or 1982 cm-1 and lie on the correlation line of v(Fe-CO) vs v(C-O) for all known five-coordinate heme Fe-CO complexes. The loss of intensity of the heme Fe-His384 mode observed at 193 cm-1 in the photostationary CO-bound spectra is attributed to the loss of the non-hydrogen bonded heme Fe-His384⋯Gly359 conformer. Taken together, the data indicate that the environment of the ruptured His384 that is a part of the Q-proton pathway and leads to the highly conserved among all heme-copper oxidases, H2O pool, is disrupted upon CO binding to heme a3. | en |
dc.source | Journal of Physical Chemistry B | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-2442719036&partnerID=40&md5=f9145de01a27c8698cd40c988918a578 | |
dc.subject | Nitric oxide | en |
dc.subject | Molecules | en |
dc.subject | Iron compounds | en |
dc.subject | Quartz | en |
dc.subject | Spectroscopy | en |
dc.subject | Copper oxides | en |
dc.subject | Enzymes | en |
dc.subject | Nitrogen compounds | en |
dc.subject | Carbon monoxide | en |
dc.subject | Laser applications | en |
dc.subject | Stereochemistry | en |
dc.subject | Protons | en |
dc.subject | Spectrometers | en |
dc.subject | Binuclear center | en |
dc.subject | Biological sensors | en |
dc.subject | Cadmium compounds | en |
dc.subject | Functional implications | en |
dc.subject | Guanylate cyclase | en |
dc.subject | Mercury compounds | en |
dc.subject | Photostable heme | en |
dc.subject | Prokaryotic organisms | en |
dc.subject | Proton translocation | en |
dc.subject | Q- proton pathway | en |
dc.subject | Resonance Raman (RR) spectra | en |
dc.subject | Tellurium compounds | en |
dc.title | Detection of a photostable five-coordinate heme a3-Fe-Co species and functional implications of His384/α10 in CO-bound ba 3-cytochrome c oxidase from Thermus thermophilus | en |
dc.type | info:eu-repo/semantics/article | |
dc.description.volume | 108 | |
dc.description.issue | 18 | |
dc.description.startingpage | 5489 | |
dc.description.endingpage | 5491 | |
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 :19</p> | en |
dc.source.abbreviation | J Phys Chem B | 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 |
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