In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins
A combination of in silico methods was used to extend the 5 experimental description of the reductive nitrosylation mechanism in ferric 6 hemeproteins with the molecular details of the role of surrounding amino acids. 7 The computational strategy consisted in the estimation of potential energy 8 pro...
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ftconicet:oai:ri.conicet.gov.ar:11336/142966 2023-10-09T21:56:07+02:00 In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins Foglia, Nicolás Oscar Bari, Sara Elizabeth Estrin, Dario Ariel application/pdf http://hdl.handle.net/11336/142966 eng eng American Chemical Society info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/acs.inorgchem.9b03198 info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.inorgchem.9b03198 http://hdl.handle.net/11336/142966 Foglia, Nicolás Oscar; Bari, Sara Elizabeth; Estrin, Dario Ariel; In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins; American Chemical Society; Inorganic Chemistry; 59; 6; 3-2020; 3631-3641 0020-1669 CONICET Digital CONICET info:eu-repo/semantics/restrictedAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ heme protein DFT QM-MM reductive nitrosylation https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1021/acs.inorgchem.9b03198 2023-09-24T18:24:09Z A combination of in silico methods was used to extend the 5 experimental description of the reductive nitrosylation mechanism in ferric 6 hemeproteins with the molecular details of the role of surrounding amino acids. 7 The computational strategy consisted in the estimation of potential energy 8 profiles for the transition process associated with the interactions of the 9 coordinated N(NO) moiety with O(H2O) or O(OH−) as nucleophiles, andwith distal amino acids as proton acceptors or affecting the stability of transitionstates. We inspected the reductive nitrosylation in three representativehemeproteins -sperm whale metmyoglobin, α subunit of human methemoglobinand nitrophorin 4 of Rhodnius prolixus. For each case, classical moleculardynamics simulations were performed in order to obtain relevant reactiveconformations, and a potential energy profile for the reactive step was obtainedusing adiabatic mapping or nudged elastic band approaches at the QM/MMlevel. Specifically, we report the role of a charged Arg45 of myoglobin in destabilizing the transition state when H2O acts as nucleophile, differently to the neutral Pro43 of the hemoglobin subunit. The case of the nitrophorin is unique in that the access of the required water molecules is scarce, thus, preventing the reaction. Fil: Foglia, Nicolás Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina Fil: Bari, Sara Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ... Article in Journal/Newspaper Sperm whale CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Inorganic Chemistry 59 6 3631 3641 |
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CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
op_collection_id |
ftconicet |
language |
English |
topic |
heme protein DFT QM-MM reductive nitrosylation https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
spellingShingle |
heme protein DFT QM-MM reductive nitrosylation https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 Foglia, Nicolás Oscar Bari, Sara Elizabeth Estrin, Dario Ariel In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins |
topic_facet |
heme protein DFT QM-MM reductive nitrosylation https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
description |
A combination of in silico methods was used to extend the 5 experimental description of the reductive nitrosylation mechanism in ferric 6 hemeproteins with the molecular details of the role of surrounding amino acids. 7 The computational strategy consisted in the estimation of potential energy 8 profiles for the transition process associated with the interactions of the 9 coordinated N(NO) moiety with O(H2O) or O(OH−) as nucleophiles, andwith distal amino acids as proton acceptors or affecting the stability of transitionstates. We inspected the reductive nitrosylation in three representativehemeproteins -sperm whale metmyoglobin, α subunit of human methemoglobinand nitrophorin 4 of Rhodnius prolixus. For each case, classical moleculardynamics simulations were performed in order to obtain relevant reactiveconformations, and a potential energy profile for the reactive step was obtainedusing adiabatic mapping or nudged elastic band approaches at the QM/MMlevel. Specifically, we report the role of a charged Arg45 of myoglobin in destabilizing the transition state when H2O acts as nucleophile, differently to the neutral Pro43 of the hemoglobin subunit. The case of the nitrophorin is unique in that the access of the required water molecules is scarce, thus, preventing the reaction. Fil: Foglia, Nicolás Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina Fil: Bari, Sara Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ... |
format |
Article in Journal/Newspaper |
author |
Foglia, Nicolás Oscar Bari, Sara Elizabeth Estrin, Dario Ariel |
author_facet |
Foglia, Nicolás Oscar Bari, Sara Elizabeth Estrin, Dario Ariel |
author_sort |
Foglia, Nicolás Oscar |
title |
In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins |
title_short |
In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins |
title_full |
In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins |
title_fullStr |
In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins |
title_full_unstemmed |
In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins |
title_sort |
in silico insight into the reductive nitrosylation of ferric hemeproteins |
publisher |
American Chemical Society |
url |
http://hdl.handle.net/11336/142966 |
geographic |
Argentina |
geographic_facet |
Argentina |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/acs.inorgchem.9b03198 info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.inorgchem.9b03198 http://hdl.handle.net/11336/142966 Foglia, Nicolás Oscar; Bari, Sara Elizabeth; Estrin, Dario Ariel; In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins; American Chemical Society; Inorganic Chemistry; 59; 6; 3-2020; 3631-3641 0020-1669 CONICET Digital CONICET |
op_rights |
info:eu-repo/semantics/restrictedAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
op_doi |
https://doi.org/10.1021/acs.inorgchem.9b03198 |
container_title |
Inorganic Chemistry |
container_volume |
59 |
container_issue |
6 |
container_start_page |
3631 |
op_container_end_page |
3641 |
_version_ |
1779320593584226304 |