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
.jpg) 
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_19326203_v7_n7_p_Marcelli
Ver los metadatos del registro completo
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| oai_identifier_str | paperaa:paper_19326203_v7_n7_p_Marcelli | 
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| 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/ar2025-10-30T11:21:01Zpaperaa: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:18962025-10-30 11:21:02.769Biblioteca 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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