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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todo:paper_15206106_v114_n25_p8536_Bikiel2023-10-03T16:20:21Z Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case Bikiel, D.E. Forti, F. Boechi, L. Nardini, M. Luque, F.J. Martí, M.A. Estrin, D.A. 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 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. Fil:Bikiel, D.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Boechi, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Martí, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_15206106_v114_n25_p8536_Bikiel |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 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 |
| topic_facet |
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 |
| description |
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. |
| format |
JOUR |
| author |
Bikiel, D.E. Forti, F. Boechi, L. Nardini, M. Luque, F.J. Martí, M.A. Estrin, D.A. |
| author_facet |
Bikiel, D.E. Forti, F. Boechi, L. Nardini, M. Luque, F.J. Martí, M.A. Estrin, D.A. |
| author_sort |
Bikiel, D.E. |
| title |
Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case |
| title_short |
Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case |
| title_full |
Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case |
| title_fullStr |
Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case |
| title_full_unstemmed |
Role of heme distortion on oxygen affinity in heme proteins: The protoglobin case |
| title_sort |
role of heme distortion on oxygen affinity in heme proteins: the protoglobin case |
| url |
http://hdl.handle.net/20.500.12110/paper_15206106_v114_n25_p8536_Bikiel |
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