Please use this identifier to cite or link to this item:
https://hdl.handle.net/20.500.14279/2202
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Pinakoulaki, Eftychia | - |
dc.contributor.author | Pfitzner, Ute | - |
dc.contributor.author | Varotsis, Constantinos | - |
dc.contributor.other | Πινακουλάκη, Ευτυχία | - |
dc.contributor.other | Βαρώτσης, Κωνσταντίνος | - |
dc.date.accessioned | 2013-01-21T13:24:08Z | en |
dc.date.accessioned | 2013-05-16T06:25:26Z | - |
dc.date.accessioned | 2015-12-02T09:15:06Z | - |
dc.date.available | 2013-01-21T13:24:08Z | en |
dc.date.available | 2013-05-16T06:25:26Z | - |
dc.date.available | 2015-12-02T09:15:06Z | - |
dc.date.issued | 2003-02-25 | - |
dc.identifier.citation | Journal of biological chemistry, 2003, vol. 278, no. 21, pp.18761-18766 | en_US |
dc.identifier.issn | 00219258 | - |
dc.identifier.uri | https://hdl.handle.net/20.500.14279/2202 | - |
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_US |
dc.format | en_US | |
dc.language.iso | en | en_US |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.rights | © The American Society for Biochemistry and Molecular Biology, Inc. | en_US |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 United States | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/us/ | * |
dc.subject | Biochemistry | en_US |
dc.subject | Amino acids | en_US |
dc.subject | Denitrification | en_US |
dc.subject | Iron | en_US |
dc.subject | Oxygen | en_US |
dc.subject | Cytochrome oxidase | en_US |
dc.subject | Copper | en_US |
dc.subject | Heme | en_US |
dc.subject | Raman spectrometry | en_US |
dc.title | Direct detection of Fe(IV)=O intermediates in the cytochrome aa3 oxidase from Paracoccus denitrificans[H2O2 reaction | en_US |
dc.type | Article | en_US |
dc.affiliation | University of Crete | en |
dc.collaboration | University of Crete | en_US |
dc.subject.category | Environmental Engineering | en_US |
dc.journals | Hybrid Open Access | en_US |
dc.country | Greece | en_US |
dc.subject.field | Engineering and Technology | en_US |
dc.publication | Peer Reviewed | en_US |
dc.identifier.doi | 10.1074/jbc.M211925200 | en_US |
dc.dept.handle | 123456789/54 | en |
dc.relation.issue | 21 | en_US |
dc.relation.volume | 278 | en_US |
cut.common.academicyear | 2003-2004 | en_US |
dc.identifier.spage | 18761 | en_US |
dc.identifier.epage | 18766 | en_US |
item.openairetype | article | - |
item.cerifentitytype | Publications | - |
item.languageiso639-1 | en | - |
item.fulltext | No Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.grantfulltext | none | - |
crisitem.author.dept | Department of Chemical Engineering | - |
crisitem.author.faculty | Faculty of Geotechnical Sciences and Environmental Management | - |
crisitem.author.orcid | 0000-0003-2771-8891 | - |
crisitem.author.parentorg | Faculty of Geotechnical Sciences and Environmental Management | - |
crisitem.journal.journalissn | 1083-351X | - |
crisitem.journal.publisher | American Society for Biochemistry and Molecular Biology | - |
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