Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case

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 s...

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Autor principal: Bikiel, D.E
Otros Autores: Forti, F., Boechi, L., Nardini, M., Luque, F.J, Martí, M.A, Estrin, D.A
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: American Chemical Society 2010
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-77953993716 
024 7 |2 cas  |a heme, 14875-96-8; oxygen, 7782-44-7; porphyrin, 24869-67-8; Archaeal Proteins; Heme; Hemeproteins; Oxygen; Porphyrins 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a JPCBF 
100 1 |a Bikiel, D.E. 
245 1 0 |a Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case 
260 |b American Chemical Society  |c 2010 
270 1 0 |m Martí, M. A.; Departamento de Química Inorgánica, Analítica y Química Física/INQUIMAE-CONICET, Ciudad Universitaria, Pabellón 2, Buenos Aires, C1428EHA, Argentina; email: dario@qi.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a 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.  |l eng 
593 |a Departamento de Química Inorgánica, Analítica y Química Física/INQUIMAE-CONICET, Ciudad Universitaria, Pabellón 2, Buenos Aires, C1428EHA, Argentina 
593 |a Departament de Fisicoquímica, Institut de Biomedicina (IBUB), Universitat de Barcelona, Av. Diagonal 643, 08028 Barcelona, Spain 
593 |a Department of Biomolecular Sciences and Biotechnology, CNR-INFM, University of Milano, Milano, Italy 
593 |a Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Pabellón 2, Buenos Aires, C1428EHA, Argentina 
690 1 0 |a BINDING ENERGY 
690 1 0 |a CHEMICAL PROPERTIES 
690 1 0 |a ELECTRONIC PROPERTIES 
690 1 0 |a HEMOGLOBIN 
690 1 0 |a OXYGEN 
690 1 0 |a BINDING AFFINITIES 
690 1 0 |a BREATHING MODES 
690 1 0 |a COMPRESSION-EXPANSION 
690 1 0 |a HEME DISTORTION 
690 1 0 |a HEME GROUP 
690 1 0 |a HEME PROTEINS 
690 1 0 |a IN-PLANE DISTORTIONS 
690 1 0 |a LIGAND AFFINITY 
690 1 0 |a MACROCYCLES 
690 1 0 |a METHANOSARCINA ACETIVORANS 
690 1 0 |a OUT-OF-PLANE DISTORTIONS 
690 1 0 |a OXYGEN AFFINITY 
690 1 0 |a PORPHYRIN RINGS 
690 1 0 |a SYSTEMATIC STUDY 
690 1 0 |a PORPHYRINS 
690 1 0 |a ARCHAEAL PROTEIN 
690 1 0 |a HEME 
690 1 0 |a HEMOPROTEIN 
690 1 0 |a OXYGEN 
690 1 0 |a PORPHYRIN 
690 1 0 |a CHEMISTRY 
690 1 0 |a METABOLISM 
690 1 0 |a METHANOSARCINA 
690 1 0 |a QUANTUM THEORY 
690 1 0 |a ARCHAEAL PROTEINS 
690 1 0 |a HEME 
690 1 0 |a HEMEPROTEINS 
690 1 0 |a METHANOSARCINA 
690 1 0 |a OXYGEN 
690 1 0 |a PORPHYRINS 
690 1 0 |a QUANTUM THEORY 
700 1 |a Forti, F. 
700 1 |a Boechi, L. 
700 1 |a Nardini, M. 
700 1 |a Luque, F.J. 
700 1 |a Martí, M.A. 
700 1 |a Estrin, D.A. 
773 0 |d American Chemical Society, 2010  |g v. 114  |h pp. 8536-8543  |k n. 25  |p J Phys Chem B  |x 15206106  |w (AR-BaUEN)CENRE-5879  |t Journal of Physical Chemistry B 
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