Please use this identifier to cite or link to this item:
https://hdl.handle.net/20.500.14279/1778
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Stavrakis, Stavros | - |
dc.contributor.author | Varotsis, Constantinos | - |
dc.contributor.author | Koutsoupakis, Constantinos | - |
dc.contributor.other | Σταυράκης, Σταύρος | - |
dc.contributor.other | Βαρώτσης, Κωνσταντίνος | - |
dc.contributor.other | Κουτσουπάκης, Κωνσταντίνος | - |
dc.date.accessioned | 2013-01-21T13:41:05Z | en |
dc.date.accessioned | 2013-05-16T06:25:14Z | - |
dc.date.accessioned | 2015-12-02T09:45:32Z | - |
dc.date.available | 2013-01-21T13:41:05Z | en |
dc.date.available | 2013-05-16T06:25:14Z | - |
dc.date.available | 2015-12-02T09:45:32Z | - |
dc.date.issued | 2002-09-06 | - |
dc.identifier.citation | Journal of biological chemistry, 2002, vol. 277, no. 36, pp. 32860-32866 | en_US |
dc.identifier.issn | 00219258 | - |
dc.identifier.uri | https://hdl.handle.net/20.500.14279/1778 | - |
dc.description.abstract | We report the first evidence for the existence of the equilibrium Cu B 1+-CO species of CO-bound reduced cytochrome ba 3 from Thermus thermophilus at room temperature. The frequency of the C-O stretching mode of Cu B 1+-CO is located at 2053 cm -1 and remains unchanged in H 2O/D 2O exchanges and, between pD 5.5 and 9.7, indicating that the chemical environment does not alter the protonation state of the Cu B histidine ligands. The data and conclusions reported here are in contrast to the changes in protonation state of Cu B-His-290, reported recently (Das, T. K., Tomson, F. K., Gennis, R. B., Gordon, M., and Rousseau, D. L. (2001) Biophys. J. 80, 2039-2045 and Das, T. P., Gomes, C. M., Teixeira, M., and Rousseau, D. L. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 9591-9596). The time-resolved step-scan FTIR difference spectra indicate that the rate of decay of the transient CU B 1+-CO complex is 34.5 s -1 and rebinding to heme a 3 occurs with k 2 = 28.6 s -1. The rate of decay of the transient Cu B 1+-CO complex displays a similar time constant as the absorption changes at 1694(+)/1706(-), attributed to perturbation of the heme a 3 propionates (COOH). The ν(C-O) of the transient Cu B 1+-CO species is the same as that of the equilibrium Cu B 1+-CO species and remains unchanged in the pD range 5.5-9.7 indicating that no structural change takes place at Cu B between these states. The implications of these results with respect to proton pathways 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 | © 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 | Ligands | en_US |
dc.subject | Absorption | en_US |
dc.subject | Copper compounds | en_US |
dc.subject | Fourier transform infrared spectroscopy | en_US |
dc.subject | Protons | en_US |
dc.subject | Carbon | en_US |
dc.subject | Histidine | en_US |
dc.subject | Bacteria | en_US |
dc.title | Observation of the equilibrium Cu B-CO complex and functional implications of the transient heme a 3 propionates in cytochrome ba 3-CO from Thermus thermophilus. Fourier transform infrared (FTIR) and time-resolved step-scan FTIR studies | 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.identifier.doi | 10.1074/jbc.M204943200 | 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 | 32860 | en_US |
dc.identifier.epage | 32866 | en_US |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
item.grantfulltext | none | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
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.dept | Department of Chemical Engineering | - |
crisitem.author.faculty | Faculty of Geotechnical Sciences and Environmental Management | - |
crisitem.author.faculty | Faculty of Geotechnical Sciences and Environmental Management | - |
crisitem.author.orcid | 0000-0003-2771-8891 | - |
crisitem.author.orcid | 0000-0001-9301-1021 | - |
crisitem.author.parentorg | Faculty of Geotechnical Sciences and Environmental Management | - |
crisitem.author.parentorg | Faculty of Geotechnical Sciences and Environmental Management | - |
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