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Bikiel, D.E.; Forti, F.; Boechi, L.; Nardini, M.; Luque, F.J.; Martí, M.A.; Estrin, D.A. "Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case" (2010) Journal of Physical Chemistry B. 114(25):8536-8543
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Abstract:

The chemical properties of heme proteins largely reflect the electronic properties of their heme group. Often, the porphyrin ring of the heme exhibits significant distortions from its isolated structure, but the impact of these distortions on the chemical properties of the heme is yet uncertain. A systematic study focused on the effects of the distortion of the macrocycle on the binding affinity for oxygen is presented. The results show that out-of-plane distortions decrease the binding affinity, while in-plane distortions can increase or decrease it. Among in-plane distortions, only the breathing mode, which involves the symmetric compression-expansion of the porphyrin ring, strongly modulates the binding affinity. These findings shed light into the peculiar binding affinity of Methanosarcina acetivorans protoglobin, a protein that contains a highly distorted heme. Overall, the results highlight that in-plane distortions might be exploited by certain classes of heme proteins to modulate the ligand affinity. © 2010 American Chemical Society.

Registro:

Documento: Artículo
Título:Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case
Autor:Bikiel, D.E.; Forti, F.; Boechi, L.; Nardini, M.; Luque, F.J.; Martí, M.A.; Estrin, D.A.
Filiación:Departamento de Química Inorgánica, Analítica y Química Física/INQUIMAE-CONICET, Ciudad Universitaria, Pabellón 2, Buenos Aires, C1428EHA, Argentina
Departament de Fisicoquímica, Institut de Biomedicina (IBUB), Universitat de Barcelona, Av. Diagonal 643, 08028 Barcelona, Spain
Department of Biomolecular Sciences and Biotechnology, CNR-INFM, University of Milano, Milano, Italy
Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Pabellón 2, Buenos Aires, C1428EHA, Argentina
Palabras clave:Binding energy; Chemical properties; Electronic properties; Hemoglobin; Oxygen; Binding affinities; Breathing modes; Compression-expansion; Heme distortion; Heme group; Heme proteins; In-plane distortions; Ligand affinity; Macrocycles; Methanosarcina acetivorans; Out-of-plane distortions; Oxygen affinity; Porphyrin rings; Systematic study; Porphyrins; archaeal protein; heme; hemoprotein; oxygen; porphyrin; chemistry; metabolism; Methanosarcina; quantum theory; Archaeal Proteins; Heme; Hemeproteins; Methanosarcina; Oxygen; Porphyrins; Quantum Theory
Año:2010
Volumen:114
Número:25
Página de inicio:8536
Página de fin:8543
DOI: http://dx.doi.org/10.1021/jp102135p
Título revista:Journal of Physical Chemistry B
Título revista abreviado:J Phys Chem B
ISSN:15206106
CODEN:JPCBF
CAS:heme, 14875-96-8; oxygen, 7782-44-7; porphyrin, 24869-67-8; Archaeal Proteins; Heme; Hemeproteins; Oxygen; Porphyrins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v114_n25_p8536_Bikiel

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Citas:

---------- APA ----------
Bikiel, D.E., Forti, F., Boechi, L., Nardini, M., Luque, F.J., Martí, M.A. & Estrin, D.A. (2010) . Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case. Journal of Physical Chemistry B, 114(25), 8536-8543.
http://dx.doi.org/10.1021/jp102135p
---------- CHICAGO ----------
Bikiel, D.E., Forti, F., Boechi, L., Nardini, M., Luque, F.J., Martí, M.A., et al. "Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case" . Journal of Physical Chemistry B 114, no. 25 (2010) : 8536-8543.
http://dx.doi.org/10.1021/jp102135p
---------- MLA ----------
Bikiel, D.E., Forti, F., Boechi, L., Nardini, M., Luque, F.J., Martí, M.A., et al. "Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case" . Journal of Physical Chemistry B, vol. 114, no. 25, 2010, pp. 8536-8543.
http://dx.doi.org/10.1021/jp102135p
---------- VANCOUVER ----------
Bikiel, D.E., Forti, F., Boechi, L., Nardini, M., Luque, F.J., Martí, M.A., et al. Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case. J Phys Chem B. 2010;114(25):8536-8543.
http://dx.doi.org/10.1021/jp102135p