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spelling paper:paper_00027863_v130_n5_p1688_Marti2023-06-08T14:22:45Z Mechanism of product release in NO detoxification from Mycobacterium tuberculosis truncated hemoglobin N Martí, Marcelo Adrián Crespo, Alejandro Estrin, Dario Ariel Eggression pathway Heme cavity Mycobacterium tuberculosis Detoxification Hemoglobin Hydration Nitric oxide Quantum chemistry Bacteria heme hemoglobin hemoglobin n nitric oxide nitrite oxygen unclassified drug article bacterial growth hydration latent period macrophage molecular dynamics molecular mechanics Mycobacterium tuberculosis nonhuman quantum chemistry quantum mechanics reaction analysis simulation stress Anions Binding Sites Computer Simulation Hemoglobins, Abnormal Ligands Models, Molecular Mycobacterium tuberculosis Nitrates Nitric Oxide Protein Binding Protein Structure, Tertiary Water The capability of Mycobacterium tuberculosis to rest in latency in the infected organism appears to be related to the disposal of detoxification mechanisms, which converts the nitric oxide (NO) produced by macrophages during the initial growth infection stage into a nitrate anion. Such a reaction appears to be associated with the truncated hemoglobin N (trHbN). Even though previous experimental and theoretical studies have examined the pathways used by NO and O2 to access the heme cavity, the eggression pathway of the nitrate anion is still a challenging question. In this work we present results obtained by means of classical and quantum chemistry simulations that show that trHbN is able to release rapidly the nitrate anion using an eggression pathway other than those used for the entry of both O2 and NO and that its release is promoted by hydration of the heme cavity. These results provide a detailed understanding of the molecular basis of the NO detoxification mechanism used by trHbN to guarantee an efficient NO detoxification and thus warrant survival of the microorganism under stress conditions. © 2008 American Chemical Society. Fil:Martí, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Crespo, 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. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v130_n5_p1688_Marti http://hdl.handle.net/20.500.12110/paper_00027863_v130_n5_p1688_Marti
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Eggression pathway
Heme cavity
Mycobacterium tuberculosis
Detoxification
Hemoglobin
Hydration
Nitric oxide
Quantum chemistry
Bacteria
heme
hemoglobin
hemoglobin n
nitric oxide
nitrite
oxygen
unclassified drug
article
bacterial growth
hydration
latent period
macrophage
molecular dynamics
molecular mechanics
Mycobacterium tuberculosis
nonhuman
quantum chemistry
quantum mechanics
reaction analysis
simulation
stress
Anions
Binding Sites
Computer Simulation
Hemoglobins, Abnormal
Ligands
Models, Molecular
Mycobacterium tuberculosis
Nitrates
Nitric Oxide
Protein Binding
Protein Structure, Tertiary
Water
spellingShingle Eggression pathway
Heme cavity
Mycobacterium tuberculosis
Detoxification
Hemoglobin
Hydration
Nitric oxide
Quantum chemistry
Bacteria
heme
hemoglobin
hemoglobin n
nitric oxide
nitrite
oxygen
unclassified drug
article
bacterial growth
hydration
latent period
macrophage
molecular dynamics
molecular mechanics
Mycobacterium tuberculosis
nonhuman
quantum chemistry
quantum mechanics
reaction analysis
simulation
stress
Anions
Binding Sites
Computer Simulation
Hemoglobins, Abnormal
Ligands
Models, Molecular
Mycobacterium tuberculosis
Nitrates
Nitric Oxide
Protein Binding
Protein Structure, Tertiary
Water
Martí, Marcelo Adrián
Crespo, Alejandro
Estrin, Dario Ariel
Mechanism of product release in NO detoxification from Mycobacterium tuberculosis truncated hemoglobin N
topic_facet Eggression pathway
Heme cavity
Mycobacterium tuberculosis
Detoxification
Hemoglobin
Hydration
Nitric oxide
Quantum chemistry
Bacteria
heme
hemoglobin
hemoglobin n
nitric oxide
nitrite
oxygen
unclassified drug
article
bacterial growth
hydration
latent period
macrophage
molecular dynamics
molecular mechanics
Mycobacterium tuberculosis
nonhuman
quantum chemistry
quantum mechanics
reaction analysis
simulation
stress
Anions
Binding Sites
Computer Simulation
Hemoglobins, Abnormal
Ligands
Models, Molecular
Mycobacterium tuberculosis
Nitrates
Nitric Oxide
Protein Binding
Protein Structure, Tertiary
Water
description The capability of Mycobacterium tuberculosis to rest in latency in the infected organism appears to be related to the disposal of detoxification mechanisms, which converts the nitric oxide (NO) produced by macrophages during the initial growth infection stage into a nitrate anion. Such a reaction appears to be associated with the truncated hemoglobin N (trHbN). Even though previous experimental and theoretical studies have examined the pathways used by NO and O2 to access the heme cavity, the eggression pathway of the nitrate anion is still a challenging question. In this work we present results obtained by means of classical and quantum chemistry simulations that show that trHbN is able to release rapidly the nitrate anion using an eggression pathway other than those used for the entry of both O2 and NO and that its release is promoted by hydration of the heme cavity. These results provide a detailed understanding of the molecular basis of the NO detoxification mechanism used by trHbN to guarantee an efficient NO detoxification and thus warrant survival of the microorganism under stress conditions. © 2008 American Chemical Society.
author Martí, Marcelo Adrián
Crespo, Alejandro
Estrin, Dario Ariel
author_facet Martí, Marcelo Adrián
Crespo, Alejandro
Estrin, Dario Ariel
author_sort Martí, Marcelo Adrián
title Mechanism of product release in NO detoxification from Mycobacterium tuberculosis truncated hemoglobin N
title_short Mechanism of product release in NO detoxification from Mycobacterium tuberculosis truncated hemoglobin N
title_full Mechanism of product release in NO detoxification from Mycobacterium tuberculosis truncated hemoglobin N
title_fullStr Mechanism of product release in NO detoxification from Mycobacterium tuberculosis truncated hemoglobin N
title_full_unstemmed Mechanism of product release in NO detoxification from Mycobacterium tuberculosis truncated hemoglobin N
title_sort mechanism of product release in no detoxification from mycobacterium tuberculosis truncated hemoglobin n
publishDate 2008
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v130_n5_p1688_Marti
http://hdl.handle.net/20.500.12110/paper_00027863_v130_n5_p1688_Marti
work_keys_str_mv AT martimarceloadrian mechanismofproductreleaseinnodetoxificationfrommycobacteriumtuberculosistruncatedhemoglobinn
AT crespoalejandro mechanismofproductreleaseinnodetoxificationfrommycobacteriumtuberculosistruncatedhemoglobinn
AT estrindarioariel mechanismofproductreleaseinnodetoxificationfrommycobacteriumtuberculosistruncatedhemoglobinn
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