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Scherlis, D.A.; Martí, M.A.; Ordejón, P.; Estrin, D.A. "Environment effects on chemical reactivity of heme proteins" (2002) International Journal of Quantum Chemistry. 90(4-5):1505-1514
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Abstract:

Heme proteins are involved in a variety of physiological processes, such as O 2 transport, electron transfer, sensing of O 2 or CO, and catalysis of redox reactions. Despite the differences in biologic function, all these proteins have iron protoporphyrin IX (heine b) as the active site. The amino acids surrounding the active site are responsible for the specific reactivity of each protein. We analyzed the environment effects on binding of small ligands such as O 2 and NO to several heine proteins using density functional theory (DFT) calculations of model systems including selected amino acid residues, and also DFT calculations of the active site coupled to an electrostatic representation of the rest of the protein. Specifically, we considered the following problems: (1) the mechanisms underlying inactivation by nitric oxide of cytochrome P450; (2) O 2 affinity of human and Ascaris hemoglobin and the role of oxygen hydrogen bonding to the distal amino acids; (3) the influence of the amino acid residues surrounding the proximal histidine in the Fe-histidine bond cleavage upon binding of NO in FixL, horseradish peroxidase, and human hemoglobin. © 2002 Wiley Periodicals, Inc. Int. J. Quantum Chem. 90.

Registro:

Documento: Artículo
Título:Environment effects on chemical reactivity of heme proteins
Autor:Scherlis, D.A.; Martí, M.A.; Ordejón, P.; Estrin, D.A.
Filiación:Departamento de Química Inorgánica, Analítica y Química-Física and INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria-Pab II, Buenos Aires, C1428EHA, Argentina
Institut de Ciencia de Materials de Barcelona—CSIC, Campus de la U.A.B., Barcelona, Bellaterra, 08193, Spain
Palabras clave:Amino acid residues; Binding of small ligands; Cytochrome P450; DFT calculations; Heme proteins; Histidine; Amino acids; Chemical reactions; Electron transitions; Porphyrins; Redox reactions; Histidine; Hemoglobin
Año:2002
Volumen:90
Número:4-5
Página de inicio:1505
Página de fin:1514
DOI: http://dx.doi.org/10.1002/qua.10361
Título revista:International Journal of Quantum Chemistry
Título revista abreviado:Int J Quantum Chem
ISSN:00207608
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207608_v90_n4-5_p1505_Scherlis

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Citas:

---------- APA ----------
Scherlis, D.A., Martí, M.A., Ordejón, P. & Estrin, D.A. (2002) . Environment effects on chemical reactivity of heme proteins. International Journal of Quantum Chemistry, 90(4-5), 1505-1514.
http://dx.doi.org/10.1002/qua.10361
---------- CHICAGO ----------
Scherlis, D.A., Martí, M.A., Ordejón, P., Estrin, D.A. "Environment effects on chemical reactivity of heme proteins" . International Journal of Quantum Chemistry 90, no. 4-5 (2002) : 1505-1514.
http://dx.doi.org/10.1002/qua.10361
---------- MLA ----------
Scherlis, D.A., Martí, M.A., Ordejón, P., Estrin, D.A. "Environment effects on chemical reactivity of heme proteins" . International Journal of Quantum Chemistry, vol. 90, no. 4-5, 2002, pp. 1505-1514.
http://dx.doi.org/10.1002/qua.10361
---------- VANCOUVER ----------
Scherlis, D.A., Martí, M.A., Ordejón, P., Estrin, D.A. Environment effects on chemical reactivity of heme proteins. Int J Quantum Chem. 2002;90(4-5):1505-1514.
http://dx.doi.org/10.1002/qua.10361