Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/6619
DC FieldValueLanguage
dc.contributor.authorPinakoulaki, Eftychia-
dc.contributor.authorYoshimura, Hideaki-
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.otherΠινακουλάκη, Ευτυχία-
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.issued2006-06-
dc.identifier.citationBiochemistry, 2006, vol. 45, no. 25, pp. 7763-7766en_US
dc.identifier.issn0006-2960-
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_US
dc.formatPdfen_US
dc.language.isoenen_US
dc.publisherACS Publicationsen
dc.relation.ispartofBiochemistryen_US
dc.rights© American Chemical Societyen_US
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/us/*
dc.subjectFourier transform infrared spectroscopyen_US
dc.subjectHydrogen bondingen_US
dc.subjectMolecular structureen_US
dc.subjectOxygenen_US
dc.subjectProteinsen_US
dc.subjectTransducersen_US
dc.subjectHemeen_US
dc.subjectAmino acid sequenceen_US
dc.titleRecognition and discrimination of gases by the oxygen-sensing signal transducer protein HemAT as revealed by FTIR spectroscopyen_US
dc.typeArticleen_US
dc.affiliationCyprus University of Technologyen
dc.collaborationUniversity of Creteen_US
dc.journalsOpen Accessen_US
dc.countrycyprusen_US
dc.subject.fieldEngineering and Technologyen_US
dc.publicationPeer Revieweden_US
dc.identifier.doi10.1021/bi0604072en_US
dc.dept.handle123456789/54en
dc.relation.issue25en_US
dc.relation.volume45en_US
cut.common.academicyear2006-2007en_US
dc.identifier.spage7763en_US
dc.identifier.epage7766en_US
item.grantfulltextnone-
item.fulltextNo Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.openairetypearticle-
item.languageiso639-1en-
item.cerifentitytypePublications-
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-
Appears in Collections:Άρθρα/Articles
CORE Recommender
Show simple item record

SCOPUSTM   
Citations 50

21
checked on Jun 22, 2020

WEB OF SCIENCETM
Citations 50

23
Last Week
0
Last month
checked on Jun 18, 2020

Page view(s) 50

194
Last Week
2
Last month
6
checked on Jun 26, 2020

Google ScholarTM

Check

Altmetric


This item is licensed under a Creative Commons License Creative Commons