dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.contributor.author | Pfitzner, U. | en |
dc.contributor.author | Ludwig, B. | en |
dc.contributor.author | Varotsis, Constantinos | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.creator | Pfitzner, U. | en |
dc.creator | Ludwig, B. | en |
dc.creator | Varotsis, Constantinos | en |
dc.date.accessioned | 2019-11-21T06:22:20Z | |
dc.date.available | 2019-11-21T06:22:20Z | |
dc.date.issued | 2003 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/56031 | |
dc.description.abstract | We report the first evidence for the formation of the "607- and 580-nm forms" in the cytochrome oxidase aa3/H2O2 reaction without the involvement of tyrosine 280. The pKa of the 607-580-nm transition is 7.5. The 607-nm form is also formed in the mixed valence cytochrome oxidase/O2 reaction in the absence of tyrosine 280. Steady-state resonance Raman characterization of the reaction products of both the wild-type and Y280H cytochrome aa3 from Paracoccus denitrificans indicate the formation of six-coordinate low spin species, and do not support, in contrast to previous reports, the formation of a porphyrin π-cation radical. We observe three oxygen isotope-sensitive Raman bands in the oxidized wild-type aa3/H2O2 reaction at 804, 790, and 358 cm-1. The former two are assigned to the Fe(IV)=O stretching mode of the 607- and 580-nm forms, respectively. The 14 cm-1 frequency difference between the oxoferryl species is attributed to variations in the basicity of the proximal to heme a3 His-411, induced by the oxoferryl conformations of the heme a3-CuB pocket during the 607-580-nm transition. We suggest that the 804-790 cm-1 oxoferryl transition triggers distal conformational changes that are subsequently communicated to the proximal His-411 heme a3 site. The 358 cm-1 mode has been found for the first time to accumulate with the 804 cm-1 mode in the peroxide reaction. These results indicate that the mechanism of oxygen reduction must be reexamined. | en |
dc.source | Journal of Biological Chemistry | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038482073&doi=10.1074%2fjbc.M211925200&partnerID=40&md5=a6f4927a92c3ac99d87e7689544d5376 | |
dc.subject | article | en |
dc.subject | controlled study | en |
dc.subject | priority journal | en |
dc.subject | unclassified drug | en |
dc.subject | nonhuman | en |
dc.subject | metabolism | en |
dc.subject | steady state | en |
dc.subject | chemistry | en |
dc.subject | Iron | en |
dc.subject | enzymology | en |
dc.subject | Oxygen | en |
dc.subject | Raman scattering | en |
dc.subject | oxidation reduction reaction | en |
dc.subject | Oxidation-Reduction | en |
dc.subject | Reduction | en |
dc.subject | copper | en |
dc.subject | pH | en |
dc.subject | Hydrogen-Ion Concentration | en |
dc.subject | cation | en |
dc.subject | coordination compound | en |
dc.subject | Biochemistry | en |
dc.subject | Negibacteria | en |
dc.subject | tyrosine | en |
dc.subject | binding site | en |
dc.subject | conformational transition | en |
dc.subject | alkalinity | en |
dc.subject | radical | en |
dc.subject | Denitrification | en |
dc.subject | spectrophotometry | en |
dc.subject | Raman spectrometry | en |
dc.subject | heme | en |
dc.subject | Spectrum Analysis, Raman | en |
dc.subject | Amino acids | en |
dc.subject | histidine | en |
dc.subject | Electron Transport Complex IV | en |
dc.subject | cytochrome c oxidase | en |
dc.subject | Oxygen Isotopes | en |
dc.subject | Paracoccus denitrificans | en |
dc.subject | hydrogen peroxide | en |
dc.subject | acceleration | en |
dc.subject | ferryl iron | en |
dc.subject | oxoferryl derivative | en |
dc.subject | peroxide | en |
dc.subject | pKa | en |
dc.subject | porphyrin | en |
dc.title | Direct detection of Fe(IV)=O intermediates in the cytochrome aa3 oxidase from Paracoccus denitrificans[H2O2 reaction | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1074/jbc.M211925200 | |
dc.description.volume | 278 | |
dc.description.issue | 21 | |
dc.description.startingpage | 18761 | |
dc.description.endingpage | 18766 | |
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 :27</p> | en |
dc.source.abbreviation | J.Biol.Chem. | 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 | |