Please use this identifier to cite or link to this item:
https://hdl.handle.net/20.500.14279/1762
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Pinakoulaki, Eftychia | - |
dc.contributor.author | Soulimane, Tewfik | - |
dc.contributor.author | Varotsis, Constantinos | - |
dc.contributor.other | Πινακουλάκη, Ευτυχία | - |
dc.contributor.other | Βαρώτσης, Κωνσταντίνος | - |
dc.date.accessioned | 2013-01-21T13:27:28Z | en |
dc.date.accessioned | 2013-05-16T06:25:26Z | - |
dc.date.accessioned | 2015-12-02T09:55:00Z | - |
dc.date.available | 2013-01-21T13:27:28Z | en |
dc.date.available | 2013-05-16T06:25:26Z | - |
dc.date.available | 2015-12-02T09:55:00Z | - |
dc.date.issued | 2002-09-06 | - |
dc.identifier.citation | Journal of biological chemistry, 2002, vol. 277, no. 36, pp. 32867-32874 | en_US |
dc.identifier.issn | 00219258 | - |
dc.identifier.uri | https://hdl.handle.net/20.500.14279/1762 | - |
dc.description.abstract | Fourier transform infrared (FTIR) and step-scan time-resolved FTIR difference spectra are reported for the [carbonmonoxy]cytochrome caa3 from Thermus thermophilus. A major C-O mode of heme a3 at 1958 cm-1 and two minor modes at 1967 and 1975 cm-1 (7:1:1) have been identified at room temperature and remained unchanged in H2O/D2O exchange. The observed C-O frequencies are 10 cm-1 higher than those obtained previously at 21 K (Einarsdóttir, O., Killough, P. M., Fee, J. A., and Woodruff, W. H. (1989) J. Biol. Chem. 264, 2405-2408). The time-resolved FTIR data indicate that the transient CuB1+-CO complex is formed at room temperature as revealed by the CO stretching mode at 2062 cm-1. Therefore, the caa3 enzyme is the only documented member of the heme-copper superfamily whose binuclear center consists of an a3-type heme of a β-form and a CuB atom of an α-form. These results illustrate that the properties of the binuclear center in other oxidases resulting in the α-form are not required for enzymatic activity. Dissociation of the transient CuB1+-CO complex is biphasic. The rate of decay is 2.3 x 104 s-1 (fast phase, 35%) and 36.3 s-1 (slow phase, 65%). The observed rate of rebinding to heme a3 is 34.1 s-1. The implications of these results with respect to the molecular motions that are general to the photodynamics of the binuclear center in heme-copper oxidases are discussed | 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 | 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 | Copper | en_US |
dc.subject | Enzymes | en_US |
dc.subject | Fourier transform infrared spectroscopy | en_US |
dc.subject | Dissociation | en_US |
dc.subject | Cytochrome oxidase | en_US |
dc.subject | Heme | en_US |
dc.subject | Protein binding | en_US |
dc.title | Fourier transform infrared (FTIR) and step-scan time-resolved FTIR spectroscopies reveal a unique active site in cytochrome caa3 oxidase from Thermus thermophilus | en_US |
dc.type | Article | en_US |
dc.affiliation | University of Crete | en |
dc.collaboration | University of Crete | en_US |
dc.subject.category | Chemical Sciences | en_US |
dc.journals | Hybrid Open Access | en_US |
dc.country | Greece | en_US |
dc.subject.field | Natural Sciences | en_US |
dc.publication | Peer Reviewed | en_US |
dc.identifier.doi | 10.1074/jbc.M205568200 | en_US |
dc.dept.handle | 123456789/54 | en |
dc.relation.issue | 36 | en_US |
dc.relation.volume | 277 | en_US |
cut.common.academicyear | 2002-2003 | en_US |
dc.identifier.spage | 32867 | en_US |
dc.identifier.epage | 32874 | en_US |
item.grantfulltext | none | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
item.cerifentitytype | Publications | - |
item.openairetype | article | - |
crisitem.journal.journalissn | 1083-351X | - |
crisitem.journal.publisher | American Society for Biochemistry and Molecular Biology | - |
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 | - |
Appears in Collections: | Άρθρα/Articles |
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