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https://hdl.handle.net/20.500.14279/9323
Πεδίο DC | Τιμή | Γλώσσα |
---|---|---|
dc.contributor.author | Ioannou, Androulla | - |
dc.contributor.author | Lambrou, Alexandra | - |
dc.contributor.author | Daskalakis, Vangelis | - |
dc.contributor.author | Pinakoulaki, Eftychia | - |
dc.date.accessioned | 2017-01-31T12:10:14Z | - |
dc.date.available | 2017-01-31T12:10:14Z | - |
dc.date.issued | 2017-02-01 | - |
dc.identifier.citation | Biophysical Chemistry, 2017, vol. 221, pp. 10-16 | en_US |
dc.identifier.issn | 18734200 | - |
dc.identifier.uri | https://hdl.handle.net/20.500.14279/9323 | - |
dc.description.abstract | Myoglobin (Mb) is known to react slowly with nitirite to form the green pigment by NO2− cordination to the heme Fe in the O-binding nitrito (O1[sbnd]N[dbnd]O2) mode and to the heme 2-vinyl position. Nitrite is a powerful oxidizing agent and a biological reservoir for NO that has been implicated in a variety of aerobic biological systems. Accordingly, it is important to elucidate the nature and variety of NO2− reaction mechanisms with Mb. We have performed principal component analysis (PCA, or essential dynamics) on Molecular Dynamics trajectories of all Mb[sbnd]NO2 coordination states to resolve the most important motions in the protein at 298 K. We show that the coordination or removal of NO2− to/from the heme iron is associated mainly with a motion of helix E and the coordination of NO2− to the 2-vinyl is associated with a motion of helix F and a correlated motion of helices E-F. This latter correlated motion can be attributed to the interaction of Val68 and Ile107 with the 2-nitrovinyl moiety. The resonance Raman results show that coordination of NO2− to the 2-vinyl is increased at pH 6.0 demonstrating that the amide protons in the F helix are not protected from access of solvent water and the helix F motion allows solvent access to the 2-vinyl group, without affecting the coordination to the heme Fe. | en_US |
dc.format | en_US | |
dc.language.iso | en | en_US |
dc.relation.ispartof | Biophysical Chemistry | en_US |
dc.rights | © Elsevier | en_US |
dc.subject | Heme proteins | en_US |
dc.subject | Molecular Dynamics | en_US |
dc.subject | Nitrite | en_US |
dc.subject | Raman spectroscopy | en_US |
dc.title | Coupling of helix E-F motion with the O-nitrito and 2-nitrovinyl coordination in myoglobin | en_US |
dc.type | Article | en_US |
dc.collaboration | Cyprus University of Technology | en_US |
dc.collaboration | University of Cyprus | en_US |
dc.subject.category | Agricultural Biotechnology | en_US |
dc.journals | Subscription | en_US |
dc.country | Cyprus | en_US |
dc.subject.field | Agricultural Sciences | en_US |
dc.publication | Peer Reviewed | en_US |
dc.identifier.doi | 10.1016/j.bpc.2016.11.009 | en_US |
dc.relation.volume | 221 | en_US |
cut.common.academicyear | 2016-2017 | en_US |
dc.identifier.spage | 10 | en_US |
dc.identifier.epage | 16 | en_US |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
item.grantfulltext | none | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.cerifentitytype | Publications | - |
item.openairetype | article | - |
crisitem.journal.journalissn | 0301-4622 | - |
crisitem.journal.publisher | Elsevier | - |
crisitem.author.dept | Department of Chemical Engineering | - |
crisitem.author.faculty | Faculty of Geotechnical Sciences and Environmental Management | - |
crisitem.author.orcid | 0000-0001-8870-0850 | - |
crisitem.author.parentorg | Faculty of Geotechnical Sciences and Environmental Management | - |
Εμφανίζεται στις συλλογές: | Άρθρα/Articles |
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