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Abstract:

The binding of diatomic ligands, such as O2, NO, and CO, to heme proteins is a process intimately related with their function. In this work, we analyzed by means of a combination of classical Molecular Dynamics (MD) and Hybrid Quantum-Classical (QM/MM) techniques the existence of multiple conformations in the distal site of heme proteins and their influence on oxygen affinity regulation. We considered two representative examples: soybean leghemoglobin (Lba) and Paramecium caudatum truncated hemoglobin (PcHb). The results presented in this work provide a molecular interpretation for the kinetic, structural, and mutational data that cannot be obtained by assuming a single distal conformation. © 2007 Wiley-Liss, Inc.

Registro:

Documento: Artículo
Título:Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
Autor:Martí, M.A.; Capece, L.; Bikiel, D.E.; Falcone, B.; Estrin, D.A.
Filiación:Departamento de Quimica Inorganica, Analitica Y Quimica Fisica INQUIMAE-CONICET, Facultad de Ciencias Exactas Y Naturales, Ciudad Universitaria, Buenos Aires C1428EHA, Argentina
Departamento de Quimica Inorganica, Analitica Y Quimica Fisica/INQUIMAE-CONICET, Facultad de Ciencias Exactas Y Naturales, Pabellón 2, Buenos Aires C1428EHA, Argentina
Palabras clave:Heme protein; Hydrogen bond; Ligand binding; Molecular dynamics; QM/MM; Structure; carbon monoxide; hemoglobin; leghemoglobin; nitric oxide; oxygen; article; computer simulation; enthalpy; hydrogen bond; molecular dynamics; mutation; nonhuman; oxygen affinity; Paramecium caudatum; priority journal; protein conformation; quantum chemistry; soybean; Animals; Binding Sites; Computer Simulation; Hemoglobins; Kinetics; Leghemoglobin; Models, Molecular; Oxygen; Paramecium caudatum; Plant Proteins; Protein Conformation; Protozoan Proteins; Soybeans; Glycine max; Paramecium caudatum
Año:2007
Volumen:68
Número:2
Página de inicio:480
Página de fin:487
DOI: http://dx.doi.org/10.1002/prot.21454
Título revista:Proteins: Structure, Function and Genetics
Título revista abreviado:Proteins Struct. Funct. Genet.
ISSN:08873585
CODEN:PSFGE
CAS:carbon monoxide, 630-08-0; hemoglobin, 9008-02-0; leghemoglobin, 52365-25-0, 53096-11-0; nitric oxide, 10102-43-9; oxygen, 7782-44-7; Hemoglobins; Leghemoglobin; Oxygen, 7782-44-7; Plant Proteins; Protozoan Proteins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08873585_v68_n2_p480_Marti

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Citas:

---------- APA ----------
Martí, M.A., Capece, L., Bikiel, D.E., Falcone, B. & Estrin, D.A. (2007) . Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases. Proteins: Structure, Function and Genetics, 68(2), 480-487.
http://dx.doi.org/10.1002/prot.21454
---------- CHICAGO ----------
Martí, M.A., Capece, L., Bikiel, D.E., Falcone, B., Estrin, D.A. "Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases" . Proteins: Structure, Function and Genetics 68, no. 2 (2007) : 480-487.
http://dx.doi.org/10.1002/prot.21454
---------- MLA ----------
Martí, M.A., Capece, L., Bikiel, D.E., Falcone, B., Estrin, D.A. "Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases" . Proteins: Structure, Function and Genetics, vol. 68, no. 2, 2007, pp. 480-487.
http://dx.doi.org/10.1002/prot.21454
---------- VANCOUVER ----------
Martí, M.A., Capece, L., Bikiel, D.E., Falcone, B., Estrin, D.A. Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases. Proteins Struct. Funct. Genet. 2007;68(2):480-487.
http://dx.doi.org/10.1002/prot.21454