dc.contributor.author | Ioannou, Androulla | en |
dc.contributor.author | Lambrou, Alexandra | en |
dc.contributor.author | Daskalakis, Vangelis | en |
dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.creator | Ioannou, Androulla | en |
dc.creator | Lambrou, Alexandra | en |
dc.creator | Daskalakis, Vangelis | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.date.accessioned | 2019-11-21T06:19:26Z | |
dc.date.available | 2019-11-21T06:19:26Z | |
dc.date.issued | 2017 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/55568 | |
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. © 2016 Elsevier B.V. | en |
dc.source | Biophysical chemistry | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84998534595&doi=10.1016%2fj.bpc.2016.11.009&partnerID=40&md5=f63eca565fdebec9d4a148b5bc4fdd15 | |
dc.subject | priority journal | en |
dc.subject | Article | en |
dc.subject | metabolism | en |
dc.subject | Animals | en |
dc.subject | animal | en |
dc.subject | chemistry | en |
dc.subject | simulation | en |
dc.subject | Raman spectroscopy | en |
dc.subject | reaction analysis | en |
dc.subject | pH | en |
dc.subject | Hydrogen-Ion Concentration | en |
dc.subject | protein secondary structure | en |
dc.subject | binding site | en |
dc.subject | proton | en |
dc.subject | Binding Sites | en |
dc.subject | Protein Structure, Secondary | en |
dc.subject | amide | en |
dc.subject | Raman spectrometry | en |
dc.subject | heme | en |
dc.subject | Heme proteins | en |
dc.subject | Molecular Dynamics | en |
dc.subject | Molecular Dynamics Simulation | en |
dc.subject | myoglobin | en |
dc.subject | Nitrite | en |
dc.subject | Nitrites | en |
dc.subject | nitro derivative | en |
dc.subject | principal component analysis | en |
dc.subject | Spectrum Analysis, Raman | en |
dc.subject | vinyl derivative | en |
dc.title | Coupling of helix E-F motion with the O-nitrito and 2-nitrovinyl coordination in myoglobin | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1016/j.bpc.2016.11.009 | |
dc.description.volume | 221 | |
dc.description.startingpage | 10 | |
dc.description.endingpage | 16 | |
dc.author.faculty | 002 Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Χημείας / Department of Chemistry | |
dc.type.uhtype | Article | en |
dc.source.abbreviation | Biophys.Chem. | en |
dc.contributor.orcid | Pinakoulaki, Eftychia [0000-0003-3320-6112] | |
dc.contributor.orcid | Daskalakis, Vangelis [0000-0001-8870-0850] | |
dc.gnosis.orcid | 0000-0003-3320-6112 | |
dc.gnosis.orcid | 0000-0001-8870-0850 | |