Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/6611
DC FieldValueLanguage
dc.contributor.authorSoulimane, Tewfiken
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.authorKoutsoupakis, Constantinos-
dc.contributor.otherΒαρώτσης, Κωνσταντίνος-
dc.contributor.otherΚουτσουπάκης, Κωνσταντίνος-
dc.date.accessioned2013-01-21T08:57:25Zen
dc.date.accessioned2013-05-16T06:25:17Z-
dc.date.accessioned2015-12-02T10:06:16Z-
dc.date.available2013-01-21T08:57:25Zen
dc.date.available2013-05-16T06:25:17Z-
dc.date.available2015-12-02T10:06:16Z-
dc.date.issued2003en
dc.identifier.citationJournal of the american chemical society, 2003, volume 125, issue 48, pages 14728-14732en
dc.identifier.issn00027863en
dc.identifier.urihttp://ktisis.cut.ac.cy/handle/10488/6611en
dc.description.abstractThe description of reaction regulation in enzymes responsible for activating and catalyzing small molecules (O2, NO) requires identification of ligand movement into the binding site and out of the enzyme through specific channels and docking sites. We have used time-resolved step-scan Fourier transform infrared spectroscopy on CO-photolyzed cytochrome c oxidase ba3 from T. thermophilus, which is responsible for the activation and reduction of both O2 and NO, to gain insight into the structure of ligand-binding intermediates at ambient temperature. We show that, upon dissociation, the photolyzed CO becomes trapped within a ligand docking site located near the ring A proplonate of heme a3. The 2131 cm -1 mode of the "docked" CO we have detected corresponds to the B1 state of Mb and persists for 35 μs. The release of CO from the docking site is not followed by recombination to the heme a3 Fe. Our analysis indicates that this behavior reflects a mechanism in which the protein near ring A of heme a3propionate reorganizes about the released CO from the docking site, and establishes a transient barrier that inhibits the recombination process to the heme a3 Fe for a few milliseconds. Rebinding to heme a3 occurs with k2 = 29.5 s-1. These results have implications for understanding the role of ligand binding/escape through docking sites and channels in heme-copper oxidases and, thus, in respirationen
dc.language.isoenen
dc.publisherACS Publicationsen
dc.rightsCopyright © 2003 American Chemical Societyen
dc.subjectEnzymesen
dc.subjectCatalysisen
dc.subjectFourier transform infrared spectroscopyen
dc.subjectLigand binding (Biochemistry)en
dc.subjectCarbon monoxideen
dc.subjectCytochrome oxidaseen
dc.subjectHemeen
dc.subjectDissociationen
dc.titleLigand binding in a docking site of cytochrome c oxidase: a time-resolved step-scan fourier transform infrared studyen
dc.typeArticleen
dc.affiliationUniversity of Creteen
dc.identifier.doi10.1021/ja036107een
dc.dept.handle123456789/54en
item.languageiso639-1other-
item.fulltextNo Fulltext-
item.grantfulltextnone-
crisitem.author.deptDepartment of Environmental Science and Technology-
crisitem.author.deptDepartment of Environmental Science and Technology-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.orcid0000-0003-2771-8891-
crisitem.author.orcid0000-0001-9301-1021-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
Appears in Collections:Άρθρα/Articles
Show simple item record

SCOPUSTM   
Citations

42
checked on Dec 16, 2018

WEB OF SCIENCETM
Citations

42
checked on Oct 16, 2019

Page view(s)

114
Last Week
14
Last month
8
checked on Oct 22, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.