Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
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 fo...
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| Formato: | Artículo publishedVersion |
| Lenguaje: | Inglés |
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2012
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_19326203_v7_n7_p_Marcelli |
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paperaa:paper_19326203_v7_n7_p_Marcelli2023-06-12T16:51:40Z Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca PLoS ONE 2012;7(7) 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. 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 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. 2012 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_19326203_v7_n7_p_Marcelli |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| language |
Inglés |
| orig_language_str_mv |
eng |
| 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 |
| spellingShingle |
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 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. Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca |
| topic_facet |
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 |
| 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. |
| format |
Artículo Artículo publishedVersion |
| author |
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_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_sort |
Marcelli, A. |
| title |
Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from 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 |
| publishDate |
2012 |
| url |
http://hdl.handle.net/20.500.12110/paper_19326203_v7_n7_p_Marcelli |
| work_keys_str_mv |
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