Please use this identifier to cite or link to this item:
https://hdl.handle.net/20.500.14279/1049
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Vamvouka, Magdalini | - |
dc.contributor.author | Varotsis, Constantinos | - |
dc.contributor.other | Βάμβουκα, Μαγδαληνή | - |
dc.contributor.other | Βαρώτσης, Κωνσταντίνος | - |
dc.date.accessioned | 2013-01-22T15:50:23Z | en |
dc.date.accessioned | 2013-05-16T06:25:27Z | - |
dc.date.accessioned | 2015-12-02T08:43:23Z | - |
dc.date.available | 2013-01-22T15:50:23Z | en |
dc.date.available | 2013-05-16T06:25:27Z | - |
dc.date.available | 2015-12-02T08:43:23Z | - |
dc.date.issued | 1998-09-09 | - |
dc.identifier.citation | Journal of Physical Chemistry B, 1998, vol. 102, no. 39, pp. 7670-7673 | en_US |
dc.identifier.issn | 10895647 | - |
dc.identifier.uri | https://hdl.handle.net/20.500.14279/1049 | - |
dc.description.abstract | Resonance 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 CuB | en_US |
dc.language.iso | en | en_US |
dc.relation.ispartof | Journal of Physical Chemistry B | en_US |
dc.rights | © American Chemical Society | en_US |
dc.subject | Fourier transform infrared spectroscopy | en_US |
dc.subject | Carbon | en_US |
dc.subject | Cytochrome oxidase | en_US |
dc.subject | Bacillus subtilis | en_US |
dc.subject | Heme | en_US |
dc.subject | Ligands | en_US |
dc.subject | Chemistry | en_US |
dc.title | Resonance raman and FTIR studies of carbon monoxide-bound cytochrome aa3-600 oxidase of bacillus subtilis | en_US |
dc.type | Article | en_US |
dc.affiliation | University of Crete | en |
dc.collaboration | University of Crete | en_US |
dc.journals | Subscription | en_US |
dc.country | Greece | en_US |
dc.subject.field | Engineering and Technology | en_US |
dc.identifier.doi | 10.1021/jp9824095 | en_US |
dc.dept.handle | 123456789/54 | en |
dc.relation.issue | 39 | en_US |
dc.relation.volume | 102 | en_US |
cut.common.academicyear | 1998-1999 | en_US |
dc.identifier.spage | 7670 | en_US |
dc.identifier.epage | 7673 | 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 | 1520-5207 | - |
crisitem.journal.publisher | American Chemical Society | - |
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