Environment effects on chemical reactivity of heme proteins
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 a...
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2002
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207608_v90_n4-5_p1505_Scherlis http://hdl.handle.net/20.500.12110/paper_00207608_v90_n4-5_p1505_Scherlis |
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paper:paper_00207608_v90_n4-5_p1505_Scherlis2023-06-08T14:41:45Z Environment effects on chemical reactivity of heme proteins Martí, Marcelo Adrián Estrin, Dario Ariel 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 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. 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. 2002 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207608_v90_n4-5_p1505_Scherlis http://hdl.handle.net/20.500.12110/paper_00207608_v90_n4-5_p1505_Scherlis |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Martí, Marcelo Adrián Estrin, Dario Ariel Environment effects on chemical reactivity of heme proteins |
| topic_facet |
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 |
| description |
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. |
| author |
Martí, Marcelo Adrián Estrin, Dario Ariel |
| author_facet |
Martí, Marcelo Adrián Estrin, Dario Ariel |
| author_sort |
Martí, Marcelo Adrián |
| title |
Environment effects on chemical reactivity of heme proteins |
| title_short |
Environment effects on chemical reactivity of heme proteins |
| title_full |
Environment effects on chemical reactivity of heme proteins |
| title_fullStr |
Environment effects on chemical reactivity of heme proteins |
| title_full_unstemmed |
Environment effects on chemical reactivity of heme proteins |
| title_sort |
environment effects on chemical reactivity of heme proteins |
| publishDate |
2002 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00207608_v90_n4-5_p1505_Scherlis http://hdl.handle.net/20.500.12110/paper_00207608_v90_n4-5_p1505_Scherlis |
| work_keys_str_mv |
AT martimarceloadrian environmenteffectsonchemicalreactivityofhemeproteins AT estrindarioariel environmenteffectsonchemicalreactivityofhemeproteins |
| _version_ |
1768545449686335488 |