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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| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
Oxford University Press
2016
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 15158caa a22013217a 4500 | ||
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| 003 | AR-BaUEN | ||
| 005 | 20230518204646.0 | ||
| 008 | 190411s2016 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-84976511301 | |
| 024 | 7 | |2 cas |a oxygen, 7782-44-7; Hemeproteins; Ligands; Oxygen; Truncated Hemoglobins | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a BOINF | ||
| 100 | 1 | |a Bustamante, J.P. | |
| 245 | 1 | 2 | |a A quantitative model for oxygen uptake and release in a family of hemeproteins |
| 260 | |b Oxford University Press |c 2016 | ||
| 270 | 1 | 0 | |m Boechi, L.; Instituto de Cálculo, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos AiresArgentina; email: lboechi@ic.fcen.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a 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. |l eng | |
| 593 | |a Departamento de Química Inorgánica, Analítica y Química Física, INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad De Buenos Aires, Argentina | ||
| 593 | |a Instituto de Cálculo, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina | ||
| 593 | |a Departamento de Matemática, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina | ||
| 593 | |a Depto. de Quim. Biol. e Inst. de Quimica Biologica de la Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a HEMOPROTEIN |
| 690 | 1 | 0 | |a LIGAND |
| 690 | 1 | 0 | |a OXYGEN |
| 690 | 1 | 0 | |a TRUNCATED HEMOGLOBIN |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a METABOLISM |
| 690 | 1 | 0 | |a HEMEPROTEINS |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a LIGANDS |
| 690 | 1 | 0 | |a OXYGEN |
| 690 | 1 | 0 | |a TRUNCATED HEMOGLOBINS |
| 700 | 1 | |a Szretter, M.E. | |
| 700 | 1 | |a Sued, M. | |
| 700 | 1 | |a Martí, M.A. | |
| 700 | 1 | |a Estrin, D.A. | |
| 700 | 1 | |a Boechi, L. | |
| 773 | 0 | |d Oxford University Press, 2016 |g v. 32 |h pp. 1805-1813 |k n. 12 |p Bioinformatics |x 13674803 |t Bioinformatics | |
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