Artículo

Capece, L.; Marti, M.A.; Crespo, A.; Doctorovich, F.; Estrin, D.A. "Heme protein oxygen affinity regulation exerted by proximal effects" (2006) Journal of the American Chemical Society. 128(38):12455-12461
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Abstract:

Heme proteins are found in all living organisms and are capable of performing a wide variety of tasks, requiring in many cases the binding of diatomic ligands, namely, O2, CO, and/or NO. Therefore, subtle regulation of these diatomic ligands' affinity is one of the key issues for determining a heme protein's function. This regulation is achieved through direct H-bond interactions between the bound ligand and the protein, and by subtle tuning of the intrinsic heme group reactivity. In this work, we present an investigation of the proximal regulation of oxygen affinity in Fe(II) histidine coordinated heme proteins by means of computer simulation. Density functional theory calculations on heme model systems are used to analyze three proximal effects: charge donation, rotational position, and distance to the heme porphyrin plane of the proximal histidine. In addition, hybrid quantum-classical (QM-MM) calculations were performed in two representative proteins: myoglobin and leghemoglobin. Our results show that all three effects are capable of tuning the Fe-O2 bond strength in a cooperative way, consistently with the experimental data on oxygen affinity. The proximal effects described herein could operate in a large variety of O2-binding heme proteins-in combination with distal effects-and are essential to understand the factors determining a heme protein's O2 affinity. © 2006 American Chemical Society.

Registro:

Documento: Artículo
Título:Heme protein oxygen affinity regulation exerted by proximal effects
Autor:Capece, L.; Marti, M.A.; Crespo, A.; Doctorovich, F.; Estrin, D.A.
Filiación:Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EHA, Argentina
Palabras clave:Hemoglobin; Hydrogen bonds; Oxygen; Probability density function; Quantum theory; Density functional theory; Heme proteins; Ligands; Oxygen affinity; Proteins; carbon monoxide; hemoprotein; histidine derivative; iron derivative; leghemoglobin; myoglobin; nitric oxide; oxygen; porphyrin; article; binding affinity; calculation; computer simulation; density functional theory; hydrogen bond; ligand binding; oxygen affinity; protein binding; protein function; Binding Sites; Computer Simulation; Ferrous Compounds; Histidine; Kinetics; Leghemoglobin; Models, Molecular; Myoglobin; Oxygen; Quantum Theory; Thermodynamics
Año:2006
Volumen:128
Número:38
Página de inicio:12455
Página de fin:12461
DOI: http://dx.doi.org/10.1021/ja0620033
Título revista:Journal of the American Chemical Society
Título revista abreviado:J. Am. Chem. Soc.
ISSN:00027863
CODEN:JACSA
CAS:carbon monoxide, 630-08-0; leghemoglobin, 52365-25-0, 53096-11-0; nitric oxide, 10102-43-9; oxygen, 7782-44-7; porphyrin, 24869-67-8; Ferrous Compounds; Histidine, 71-00-1; Leghemoglobin; Myoglobin; Oxygen, 7782-44-7
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v128_n38_p12455_Capece

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Citas:

---------- APA ----------
Capece, L., Marti, M.A., Crespo, A., Doctorovich, F. & Estrin, D.A. (2006) . Heme protein oxygen affinity regulation exerted by proximal effects. Journal of the American Chemical Society, 128(38), 12455-12461.
http://dx.doi.org/10.1021/ja0620033
---------- CHICAGO ----------
Capece, L., Marti, M.A., Crespo, A., Doctorovich, F., Estrin, D.A. "Heme protein oxygen affinity regulation exerted by proximal effects" . Journal of the American Chemical Society 128, no. 38 (2006) : 12455-12461.
http://dx.doi.org/10.1021/ja0620033
---------- MLA ----------
Capece, L., Marti, M.A., Crespo, A., Doctorovich, F., Estrin, D.A. "Heme protein oxygen affinity regulation exerted by proximal effects" . Journal of the American Chemical Society, vol. 128, no. 38, 2006, pp. 12455-12461.
http://dx.doi.org/10.1021/ja0620033
---------- VANCOUVER ----------
Capece, L., Marti, M.A., Crespo, A., Doctorovich, F., Estrin, D.A. Heme protein oxygen affinity regulation exerted by proximal effects. J. Am. Chem. Soc. 2006;128(38):12455-12461.
http://dx.doi.org/10.1021/ja0620033