Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/6545
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dc.contributor.authorVarotsis, Constantinos-
dc.contributor.authorDaskalakis, Evangelos-
dc.contributor.otherΒαρώτσης, Κωνσταντίνος-
dc.contributor.otherΔασκαλάκης, Ευάγγελος-
dc.date.accessioned2013-01-16T13:36:45Zen
dc.date.accessioned2013-05-16T06:25:24Z-
dc.date.accessioned2015-12-02T09:03:54Z-
dc.date.available2013-01-16T13:36:45Zen
dc.date.available2013-05-16T06:25:24Z-
dc.date.available2015-12-02T09:03:54Z-
dc.date.issued2009en
dc.identifier.citationInternational journal of molecular sciences, 2009, volume 10, issue 9, pages 4137-4156en
dc.identifier.issn14220067en
dc.identifier.urihttp://ktisis.cut.ac.cy/handle/10488/6545en
dc.description.abstractDynamics and reactivity in heme proteins include direct and indirect interactions of the ligands/substrates like CO, NO and O 2 with the environment. Direct electrostatic interactions result from amino acid side chains in the inner cavities and/or metal coordination in the active site, whereas indirect interactions result by ligands in the same coordination sphere. Interactions play a crucial role in stabilizing transition states in catalysis or altering ligation chemistry. We have probed, by Density Functional Theory (DFT), the perturbation degree in the stretching vibrational frequencies of CO, NO and O 2 molecules in the presence of electrostatic interactions or hydrogen bonds, under conditions simulating the inner cavities. Moreover, we have studied the vibrational characteristics of the heme bound form of the CO and NO ligands by altering the chemistry of the proximal to the heme ligand. CO, NO and O 2 molecules are highly polarizable exerting vibrational shifts up to 80, 200 and 120 cm -1, respectively, compared to the non-interacting ligand. The importance of Density Functional Theory (DFT) methodology in the investigation of the heme-ligand-protein interactions is also addresseden
dc.language.isoenen
dc.publisherMDPIen
dc.rights© 2009 by the authorsen
dc.subjectDensity functionalsen
dc.subjectCarbon monoxideen
dc.subjectHemoproteinsen
dc.subjectNitric oxideen
dc.subjectOxygenen
dc.subjectHydrogen bondingen
dc.subjectMolecular dynamicsen
dc.subjectProtein bindingen
dc.titleBinding and docking interactions of NO, CO and O 2 in heme proteins as probed by density functional theoryen
dc.typeArticleen
dc.collaborationUniversity of Crete-
dc.identifier.doi10.3390/ijms10094137en
dc.identifier.pmid19865536-
dc.dept.handle123456789/54en
item.grantfulltextopen-
item.fulltextWith Fulltext-
item.languageiso639-1other-
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.orcid0000-0001-8870-0850-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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