A quantitative model for oxygen uptake and release in a family of hemeproteins
Motivation: Hemeproteins have many diverse functions that largely depend on the rate at which they uptake or release small ligands, like oxygen. These proteins have been extensively studied using either simulations or experiments, albeit only qualitatively and one or two proteins at a time. Results:...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_13674803_v32_n12_p1805_Bustamante |
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todo:paper_13674803_v32_n12_p1805_Bustamante2023-10-03T16:11:33Z A quantitative model for oxygen uptake and release in a family of hemeproteins Bustamante, J.P. Szretter, M.E. Sued, M. Martí, M.A. Estrin, D.A. Boechi, L. hemoprotein ligand oxygen truncated hemoglobin kinetics metabolism Hemeproteins Kinetics Ligands Oxygen Truncated Hemoglobins Motivation: Hemeproteins have many diverse functions that largely depend on the rate at which they uptake or release small ligands, like oxygen. These proteins have been extensively studied using either simulations or experiments, albeit only qualitatively and one or two proteins at a time. Results: We present a physical-chemical model, which uses data obtained exclusively from computer simulations, to describe the uptake and release of oxygen in a family of hemeproteins, called truncated hemoglobins (trHbs). Through a rigorous statistical analysis we demonstrate that our model successfully recaptures all the reported experimental oxygen association and dissociation kinetic rate constants, thus allowing us to establish the key factors that determine the rates at which these hemeproteins uptake and release oxygen. We found that internal tunnels as well as the distal site water molecules control ligand uptake, whereas oxygen stabilization by distal site residues controls ligand release. Because these rates largely determine the functions of these hemeproteins, these approaches will also be important tools in characterizing the trHbs members with unknown functions. © 2016 The Author 2016. Fil:Bustamante, J.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Sued, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Martí, M.A. 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. Fil:Boechi, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13674803_v32_n12_p1805_Bustamante |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
hemoprotein ligand oxygen truncated hemoglobin kinetics metabolism Hemeproteins Kinetics Ligands Oxygen Truncated Hemoglobins |
| spellingShingle |
hemoprotein ligand oxygen truncated hemoglobin kinetics metabolism Hemeproteins Kinetics Ligands Oxygen Truncated Hemoglobins Bustamante, J.P. Szretter, M.E. Sued, M. Martí, M.A. Estrin, D.A. Boechi, L. A quantitative model for oxygen uptake and release in a family of hemeproteins |
| topic_facet |
hemoprotein ligand oxygen truncated hemoglobin kinetics metabolism Hemeproteins Kinetics Ligands Oxygen Truncated Hemoglobins |
| description |
Motivation: Hemeproteins have many diverse functions that largely depend on the rate at which they uptake or release small ligands, like oxygen. These proteins have been extensively studied using either simulations or experiments, albeit only qualitatively and one or two proteins at a time. Results: We present a physical-chemical model, which uses data obtained exclusively from computer simulations, to describe the uptake and release of oxygen in a family of hemeproteins, called truncated hemoglobins (trHbs). Through a rigorous statistical analysis we demonstrate that our model successfully recaptures all the reported experimental oxygen association and dissociation kinetic rate constants, thus allowing us to establish the key factors that determine the rates at which these hemeproteins uptake and release oxygen. We found that internal tunnels as well as the distal site water molecules control ligand uptake, whereas oxygen stabilization by distal site residues controls ligand release. Because these rates largely determine the functions of these hemeproteins, these approaches will also be important tools in characterizing the trHbs members with unknown functions. © 2016 The Author 2016. |
| format |
JOUR |
| author |
Bustamante, J.P. Szretter, M.E. Sued, M. Martí, M.A. Estrin, D.A. Boechi, L. |
| author_facet |
Bustamante, J.P. Szretter, M.E. Sued, M. Martí, M.A. Estrin, D.A. Boechi, L. |
| author_sort |
Bustamante, J.P. |
| title |
A quantitative model for oxygen uptake and release in a family of hemeproteins |
| title_short |
A quantitative model for oxygen uptake and release in a family of hemeproteins |
| title_full |
A quantitative model for oxygen uptake and release in a family of hemeproteins |
| title_fullStr |
A quantitative model for oxygen uptake and release in a family of hemeproteins |
| title_full_unstemmed |
A quantitative model for oxygen uptake and release in a family of hemeproteins |
| title_sort |
quantitative model for oxygen uptake and release in a family of hemeproteins |
| url |
http://hdl.handle.net/20.500.12110/paper_13674803_v32_n12_p1805_Bustamante |
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