Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/6642
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dc.contributor.authorVamvouka, Magdalinien
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.otherΒάμβουκα, Μαγδαληνήen
dc.contributor.otherΒαρώτσης, Κωνσταντίνος-
dc.date.accessioned2013-01-22T15:50:23Zen
dc.date.accessioned2013-05-16T06:25:27Z-
dc.date.accessioned2015-12-02T08:43:23Z-
dc.date.available2013-01-22T15:50:23Zen
dc.date.available2013-05-16T06:25:27Z-
dc.date.available2015-12-02T08:43:23Z-
dc.date.issued1998en
dc.identifier.citationJournal of physical chemistry B, 1998, volume 102, issue 39, pages 7670-7673en
dc.identifier.issn10895647en
dc.identifier.urihttp://ktisis.cut.ac.cy/handle/10488/6642en
dc.description.abstractResonance Raman and FTIR spectra are reported for the fully reduced carbon monoxy derivative of the quinol aa3-600 oxidase from Bacillus subtilis. The resonance Raman spectra display two isotope-dependent vibrational modes at 520 and 575 cm-1. The FTIR spectrum displays a single vibrational mode at 1963 cm-1. We assign the band at 520 cm-1 to the Fe-CO stretching mode, the band at 575 cm-1 to the Fe-C-O bending mode, and the band at 1963 cm-1 to the C-O stretching mode. The frequencies of these modes are similar to those that have been reported for the CO-bound mammalian cytochrome c oxidase. Despite the fact that two different heme-protein conformations that affect the iron-his bond strength are present in the ferrous ligand-free form of aa3-600, the CO-bound adduct has a single conformation in which the His-Fe-CO CUB moiety has the same structure as the α form found in the mammalian cytochrome c oxidase. The present and previous data on the vibrational frequencies of ferrous ligand-free and ferrous CO-bound forms of terminal oxidases show that an inverse linear relationship exists between the frequencies of the Fe-his and Fe-CO stretching modes. We suggest that the frequencies of both the Fe-CO and C-O modes found in heme-CUB oxidases are affected by the proximal His376, which is H-bonded to the peptide carbonyl of Gly351, and by distal effects on the heme a3-bound CO exerted by CuBen
dc.language.isoenen
dc.publisherACS Publicationsen
dc.rightsCopyright © 1998 American Chemical Societyen
dc.subjectFourier transform infrared spectroscopyen
dc.subjectCarbonen
dc.subjectCytochrome oxidaseen
dc.subjectBacillus subtilisen
dc.subjectHemeen
dc.subjectLigandsen
dc.subjectChemistryen
dc.titleResonance raman and FTIR studies of carbon monoxide-bound cytochrome aa3-600 oxidase of bacillus subtilisen
dc.typeArticleen
dc.affiliationUniversity of Creteen
dc.identifier.doi10.1021/jp9824095en
dc.dept.handle123456789/54en
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.cerifentitytypePublications-
item.languageiso639-1en-
item.openairetypearticle-
crisitem.author.deptDepartment of Chemical Engineering-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.orcid0000-0003-2771-8891-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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