Heme protein oxygen affinity regulation exerted by proximal effects

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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...

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Autor principal: Capece, L.
Otros Autores: Marti, M.A, Crespo, A., Doctorovich, F., Estrin, D.A
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2006
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-33749179197 
024 7 |2 cas  |a 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 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a JACSA 
100 1 |a Capece, L. 
245 1 0 |a Heme protein oxygen affinity regulation exerted by proximal effects 
260 |c 2006 
270 1 0 |m Estrin, D.A.; Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EHA, Argentina; email: dario@qi.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a 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.  |l eng 
593 |a Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EHA, Argentina 
690 1 0 |a HEMOGLOBIN 
690 1 0 |a HYDROGEN BONDS 
690 1 0 |a OXYGEN 
690 1 0 |a PROBABILITY DENSITY FUNCTION 
690 1 0 |a QUANTUM THEORY 
690 1 0 |a DENSITY FUNCTIONAL THEORY 
690 1 0 |a HEME PROTEINS 
690 1 0 |a LIGANDS 
690 1 0 |a OXYGEN AFFINITY 
690 1 0 |a PROTEINS 
690 1 0 |a CARBON MONOXIDE 
690 1 0 |a HEMOPROTEIN 
690 1 0 |a HISTIDINE DERIVATIVE 
690 1 0 |a IRON DERIVATIVE 
690 1 0 |a LEGHEMOGLOBIN 
690 1 0 |a MYOGLOBIN 
690 1 0 |a NITRIC OXIDE 
690 1 0 |a OXYGEN 
690 1 0 |a PORPHYRIN 
690 1 0 |a ARTICLE 
690 1 0 |a BINDING AFFINITY 
690 1 0 |a CALCULATION 
690 1 0 |a COMPUTER SIMULATION 
690 1 0 |a DENSITY FUNCTIONAL THEORY 
690 1 0 |a HYDROGEN BOND 
690 1 0 |a LIGAND BINDING 
690 1 0 |a OXYGEN AFFINITY 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN FUNCTION 
690 1 0 |a BINDING SITES 
690 1 0 |a COMPUTER SIMULATION 
690 1 0 |a FERROUS COMPOUNDS 
690 1 0 |a HISTIDINE 
690 1 0 |a KINETICS 
690 1 0 |a LEGHEMOGLOBIN 
690 1 0 |a MODELS, MOLECULAR 
690 1 0 |a MYOGLOBIN 
690 1 0 |a OXYGEN 
690 1 0 |a QUANTUM THEORY 
690 1 0 |a THERMODYNAMICS 
700 1 |a Marti, M.A. 
700 1 |a Crespo, A. 
700 1 |a Doctorovich, F. 
700 1 |a Estrin, D.A. 
773 0 |d 2006  |g v. 128  |h pp. 12455-12461  |k n. 38  |p J. Am. Chem. Soc.  |x 00027863  |w (AR-BaUEN)CENRE-19  |t Journal of the American Chemical Society 
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856 4 0 |u https://doi.org/10.1021/ja0620033  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00027863_v128_n38_p12455_Capece  |y Handle 
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