Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca

Autores
Marcelli, A.; Abbruzzetti, S.; Bustamante, J.P.; Feis, A.; Bonamore, A.; Boffi, A.; Gellini, C.; Salvi, P.R.; Estrin, D.A.; Bruno, S.; Viappiani, C.; Foggi, P.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
CO 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.
Fil:Bustamante, J.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
PLoS ONE 2012;7(7)
Materia
carbon monoxide
truncated hemoglobin
article
bacterium
binding affinity
binding kinetics
binding site
complex formation
controlled study
enthalpy
entropy
ligand binding
molecular dynamics
molecular recognition
nonhuman
photoacoustic spectroscopy
photolysis
protein binding
quantum yield
steady state
temperature sensitivity
Thermobifida fusca
Actinomycetales
Carbon Monoxide
Kinetics
Ligands
Photolysis
Protein Binding
Time Factors
Truncated Hemoglobins
Thermobifida fusca
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_19326203_v7_n7_p_Marcelli

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oai_identifier_str paperaa:paper_19326203_v7_n7_p_Marcelli
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fuscaMarcelli, A.Abbruzzetti, S.Bustamante, J.P.Feis, A.Bonamore, A.Boffi, A.Gellini, C.Salvi, P.R.Estrin, D.A.Bruno, S.Viappiani, C.Foggi, P.carbon monoxidetruncated hemoglobinarticlebacteriumbinding affinitybinding kineticsbinding sitecomplex formationcontrolled studyenthalpyentropyligand bindingmolecular dynamicsmolecular recognitionnonhumanphotoacoustic spectroscopyphotolysisprotein bindingquantum yieldsteady statetemperature sensitivityThermobifida fuscaActinomycetalesCarbon MonoxideKineticsLigandsPhotolysisProtein BindingTime FactorsTruncated HemoglobinsThermobifida fuscaCO 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.Fil:Bustamante, J.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_19326203_v7_n7_p_MarcelliPLoS ONE 2012;7(7)reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:42:57Zpaperaa:paper_19326203_v7_n7_p_MarcelliInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:42:59.014Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
title Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
spellingShingle Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
Marcelli, A.
carbon monoxide
truncated hemoglobin
article
bacterium
binding affinity
binding kinetics
binding site
complex formation
controlled study
enthalpy
entropy
ligand binding
molecular dynamics
molecular recognition
nonhuman
photoacoustic spectroscopy
photolysis
protein binding
quantum yield
steady state
temperature sensitivity
Thermobifida fusca
Actinomycetales
Carbon Monoxide
Kinetics
Ligands
Photolysis
Protein Binding
Time Factors
Truncated Hemoglobins
Thermobifida fusca
title_short Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
title_full Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
title_fullStr Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
title_full_unstemmed Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
title_sort Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
dc.creator.none.fl_str_mv Marcelli, A.
Abbruzzetti, S.
Bustamante, J.P.
Feis, A.
Bonamore, A.
Boffi, A.
Gellini, C.
Salvi, P.R.
Estrin, D.A.
Bruno, S.
Viappiani, C.
Foggi, P.
author Marcelli, A.
author_facet Marcelli, A.
Abbruzzetti, S.
Bustamante, J.P.
Feis, A.
Bonamore, A.
Boffi, A.
Gellini, C.
Salvi, P.R.
Estrin, D.A.
Bruno, S.
Viappiani, C.
Foggi, P.
author_role author
author2 Abbruzzetti, S.
Bustamante, J.P.
Feis, A.
Bonamore, A.
Boffi, A.
Gellini, C.
Salvi, P.R.
Estrin, D.A.
Bruno, S.
Viappiani, C.
Foggi, P.
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv carbon monoxide
truncated hemoglobin
article
bacterium
binding affinity
binding kinetics
binding site
complex formation
controlled study
enthalpy
entropy
ligand binding
molecular dynamics
molecular recognition
nonhuman
photoacoustic spectroscopy
photolysis
protein binding
quantum yield
steady state
temperature sensitivity
Thermobifida fusca
Actinomycetales
Carbon Monoxide
Kinetics
Ligands
Photolysis
Protein Binding
Time Factors
Truncated Hemoglobins
Thermobifida fusca
topic carbon monoxide
truncated hemoglobin
article
bacterium
binding affinity
binding kinetics
binding site
complex formation
controlled study
enthalpy
entropy
ligand binding
molecular dynamics
molecular recognition
nonhuman
photoacoustic spectroscopy
photolysis
protein binding
quantum yield
steady state
temperature sensitivity
Thermobifida fusca
Actinomycetales
Carbon Monoxide
Kinetics
Ligands
Photolysis
Protein Binding
Time Factors
Truncated Hemoglobins
Thermobifida fusca
dc.description.none.fl_txt_mv CO 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.
Fil:Bustamante, J.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description CO 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.
publishDate 2012
dc.date.none.fl_str_mv 2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_19326203_v7_n7_p_Marcelli
url http://hdl.handle.net/20.500.12110/paper_19326203_v7_n7_p_Marcelli
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv PLoS ONE 2012;7(7)
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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