Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/6619
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dc.contributor.authorPinakoulaki, Eftychiaen
dc.contributor.authorYoshimura, Hideakien
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.otherΠινακουλάκη, Ευτυχίαen
dc.contributor.otherΒαρώτσης, Κωνσταντίνος-
dc.date.accessioned2013-01-21T11:45:22Zen
dc.date.accessioned2013-05-16T06:25:19Z-
dc.date.accessioned2015-12-02T09:50:21Z-
dc.date.available2013-01-21T11:45:22Zen
dc.date.available2013-05-16T06:25:19Z-
dc.date.available2015-12-02T09:50:21Z-
dc.date.issued2006en
dc.identifier.citationBiochemistry, 2006, Volume 45, Issue 25, Pages 7763-7766en
dc.identifier.issn00062960en
dc.identifier.urihttp://ktisis.cut.ac.cy/handle/10488/6619en
dc.description.abstractThe determination of ligand binding properties is a key step in our understanding of gas sensing and discrimination by gas sensory proteins. HemAT is a newly discovered signal transducer heme protein that recognizes O 2 and discriminates against other gases such as CO and NO. We have used FTIR spectroscopy on CO- and NO-bound sensor domain HemAT and sensor domain distal mutants Y70F, T95A, R91A, and L92A to gain insight into the structure of the iron-bound ligand at ambient temperature. These mutations were designed to perturb the electrostatic field near the iron-bound gaseous ligand and also allow us to investigate the communication pathway between the distal residues of the protein and the heme. We show the formation of both H-bonded and non-H-bonded conformations in the CO-bound forms. In addition, we report the presence of multiple conformations in the NO-bound forms. Such distal H-bonding is crucial for ligand binding and activation by the heme. The comparison of the O2, NO, and CO data demonstrates that Thr95 and Tyr70 are crucial for ligand recognition and discrimination and, thus, for specific sensing of gases, and L92 is crucial for controlling the conformational changes of the Thr95 and Tyr70 residues upon NO bindingen
dc.language.isoenen
dc.publisherACS Publicationsen
dc.rights© 2006 American Chemical Societyen
dc.subjectFourier transform infrared spectroscopyen
dc.subjectHydrogen bondingen
dc.subjectMolecular structureen
dc.subjectOxygenen
dc.subjectProteinsen
dc.subjectTransducersen
dc.subjectHemeen
dc.subjectAmino acid sequenceen
dc.titleRecognition and discrimination of gases by the oxygen-sensing signal transducer protein HemAT as revealed by FTIR spectroscopyen
dc.typeArticleen
dc.affiliationCyprus University of Technologyen
dc.identifier.doi10.1021/bi0604072en
dc.dept.handle123456789/54en
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.openairetypearticle-
item.grantfulltextnone-
item.languageiso639-1en-
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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