1. RODNA
  2. FCEN
  3. FCEN - Facultad de Ciencias Exactas y Naturales. UBA
Registro completo de metadatos
Campo DC Valor Lengua/Idioma
dc.provenanceFacultad de Ciencias Exactas y Naturales de la UBA-
dc.contributorMarcelli, A.-
dc.contributorAbbruzzetti, S.-
dc.contributor<div class="autor_fcen" id="1270">Bustamante, J.P.</div>-
dc.contributorFeis, A.-
dc.contributorBonamore, A.-
dc.contributorBoffi, A.-
dc.contributorGellini, C.-
dc.contributorSalvi, P.R.-
dc.contributor<div class="autor_fcen" id="2857">Estrin, D.A.</div>-
dc.contributorBruno, S.-
dc.contributorViappiani, C.-
dc.contributorFoggi, P.-
dc.creatorMarcelli, A.-
dc.creatorAbbruzzetti, S.-
dc.creator<div class="autor_fcen" id="1270">Bustamante, J.P.</div>-
dc.creatorFeis, A.-
dc.creatorBonamore, A.-
dc.creatorBoffi, A.-
dc.creatorGellini, C.-
dc.creatorSalvi, P.R.-
dc.creator<div class="autor_fcen" id="2857">Estrin, D.A.</div>-
dc.creatorBruno, S.-
dc.creatorViappiani, C.-
dc.creatorFoggi, P.-
dc.date.accessioned2018-05-04T21:55:17Z-
dc.date.accessioned2018-05-28T15:49:20Z-
dc.date.available2018-05-04T21:55:17Z-
dc.date.available2018-05-28T15:49:20Z-
dc.date.issued2012-
dc.identifier.urihttp://10.0.0.11:8080/jspui/handle/bnmm/68633-
dc.descriptionCO recombination kinetics has been investigated in the type II truncated hemoglobin from Thermobifida fusca (Tf-trHb) over more than 10 time decades (from 1 ps to ~100 ms) by combining femtosecond transient absorption, nanosecond laser flash photolysis and optoacoustic spectroscopy. Photolysis is followed by a rapid geminate recombination with a time constant of ~2 ns representing almost 60% of the overall reaction. An additional, small amplitude geminate recombination was identified at ~100 ns. Finally, CO pressure dependent measurements brought out the presence of two transient species in the second order rebinding phase, with time constants ranging from ~3 to ~100 ms. The available experimental evidence suggests that the two transients are due to the presence of two conformations which do not interconvert within the time frame of the experiment. Computational studies revealed that the plasticity of protein structure is able to define a branched pathway connecting the ligand binding site and the solvent. This allowed to build a kinetic model capable of describing the complete time course of the CO rebinding kinetics to Tf-trHb. © 2012 Marcelli et al.-
dc.descriptionFil:Bustamante, J.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.descriptionFil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.-
dc.formatapplication/pdf-
dc.languageeng-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttp://creativecommons.org/licenses/by/2.5/ar-
dc.sourcePLoS ONE 2012;7(7)-
dc.source.urihttp://digital.bl.fcen.uba.ar/Download/paper/paper_19326203_v7_n7_p_Marcelli.pdf-
dc.subjectcarbon monoxide-
dc.subjecttruncated hemoglobin-
dc.subjectarticle-
dc.subjectbacterium-
dc.subjectbinding affinity-
dc.subjectbinding kinetics-
dc.subjectbinding site-
dc.subjectcomplex formation-
dc.subjectcontrolled study-
dc.subjectenthalpy-
dc.subjectentropy-
dc.subjectligand binding-
dc.subjectmolecular dynamics-
dc.subjectmolecular recognition-
dc.subjectnonhuman-
dc.subjectphotoacoustic spectroscopy-
dc.subjectphotolysis-
dc.subjectprotein binding-
dc.subjectquantum yield-
dc.subjectsteady state-
dc.subjecttemperature sensitivity-
dc.subjectThermobifida fusca-
dc.subjectActinomycetales-
dc.subjectCarbon Monoxide-
dc.subjectKinetics-
dc.subjectLigands-
dc.subjectPhotolysis-
dc.subjectProtein Binding-
dc.subjectTime Factors-
dc.subjectTruncated Hemoglobins-
dc.subjectThermobifida fusca-
dc.titleFollowing ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:ar-repo/semantics/artículo-
dc.typeinfo:eu-repo/semantics/publishedVersion-
Aparece en las colecciones: FCEN - Facultad de Ciencias Exactas y Naturales. UBA

Ficheros en este ítem:
No hay ficheros asociados a este ítem.
Mostrar el registro sencillo del ítem