Mechanism of product release in NO detoxification from Mycobacterium tuberculosis truncated hemoglobin N

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 ap...

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Autor principal: Martí, M.A
Otros Autores: Bidon-Chanal, A., Crespo, A., Yeh, S.-R, Guallar, V., Luque, F.J, Estrin, D.A
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2008
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-38949211777 
024 7 |2 cas  |a heme, 14875-96-8; hemoglobin, 9008-02-0; nitric oxide, 10102-43-9; nitrite, 14797-65-0; oxygen, 7782-44-7; Anions; Hemoglobins, Abnormal; Ligands; Nitrates; Nitric Oxide, 10102-43-9; Water, 7732-18-5; hemoglobins N, 9035-12-5 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a JACSA 
100 1 |a Martí, M.A. 
245 1 0 |a Mechanism of product release in NO detoxification from Mycobacterium tuberculosis truncated hemoglobin N 
260 |c 2008 
270 1 0 |m Guallar, V.; ICREA, Computacional Biology Program, Barcelona Supercomputing Center, Barcelona 08028, Spain; email: victor.guallar@bsc.es 
506 |2 openaire  |e Política editorial 
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504 |a Pathania, R., Navani, N.K., Gardner, A.M., Gardner, P.R., Dikshit, K.L., (2002) Mol. Microbiol, 45, p. 1303 
504 |a Moens, L., Vanfleteren, J., van de Peer, Y., Peeters, K., Kapp, O., Czeluzniak, J., Goodman, M., Vinogradov, S., (1996) Mol. Biol. Evol, 13, p. 324 
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504 |a Milani, M., Pesce, A., Nardini, M., Ouellet, H., Ouellet, Y., Dewilde, S., Bocedi, A., Bolognesi, M., (2005) J. Inorg. Biochem, 99, p. 97 
504 |a Milani, M., Pesce, A., Ouellet, Y., Ascenzi, P., Guertin, M., Bolognesi, M., (2001) EMBO J, 20, p. 3902 
504 |a Milani, M., Pesce, A., Ouellet, Y., Dewilde, S., Friedman, J.M., Ascenzi, P., Guertin, M., Bolognesi, M., (2004) J. Biol. Chem, 279, p. 21520 
504 |a Crespo, A., Martí, M.A., Kalko, S.G., Morreale, A., Orozco, M., Gelpí, J.L., Luque, F.J., Estrin, D.A., (2005) J. Am. Chem. Soc, 127, p. 4433 
504 |a Bidon-Chanal, A., Martí, M.A., Crespo, A., Milani, M., Orozco, M., Bolognesi, M., Luque, F.J., Estrin, D.A., (2006) Proteins, 64, p. 457 
504 |a Bidon-Chanal, A., Martí, M.A., Estrin, D.A., Luque, F.J., (2007) J. Am. Chem. Soc, 129, p. 6782 
504 |a Jorgensen, W.L., Chandrasekhar, J., Madura, J.D., Impey, R.W., Klein, M.L., (1983) J. Chem. Phys, 79, p. 926 
504 |a Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.R., Cheatham III, T.E., DeBolt, S., Ferguson, D., Kollman, P., (1995) Comp. Phys. Commun, 91, p. 1 
504 |a Jarzynski, C., (1997) Phys. Rev. Lett, 78, p. 2690 
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504 |a Kleywegt, G.J., Jones, T.A., (1994) Acta Crystallogr, D50, p. 1178 
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520 3 |a 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.  |l eng 
593 |a Departamento de Quimica Inorganica,Analitica Y Quimica Fisica/INQUIMAE-CONICET, Facultad de Ciencias Exactas Y Naturales, 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 Physiology and Biophysics, Albert Einstein College of Medicine, Yeshiva University, Bronx, NY 10461, United States 
593 |a ICREA, Computacional Biology Program, Barcelona Supercomputing Center, Barcelona 08028, Spain 
690 1 0 |a EGGRESSION PATHWAY 
690 1 0 |a HEME CAVITY 
690 1 0 |a MYCOBACTERIUM TUBERCULOSIS 
690 1 0 |a DETOXIFICATION 
690 1 0 |a HEMOGLOBIN 
690 1 0 |a HYDRATION 
690 1 0 |a NITRIC OXIDE 
690 1 0 |a QUANTUM CHEMISTRY 
690 1 0 |a BACTERIA 
690 1 0 |a HEME 
690 1 0 |a HEMOGLOBIN 
690 1 0 |a HEMOGLOBIN N 
690 1 0 |a NITRIC OXIDE 
690 1 0 |a NITRITE 
690 1 0 |a OXYGEN 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a ARTICLE 
690 1 0 |a BACTERIAL GROWTH 
690 1 0 |a HYDRATION 
690 1 0 |a LATENT PERIOD 
690 1 0 |a MACROPHAGE 
690 1 0 |a MOLECULAR DYNAMICS 
690 1 0 |a MOLECULAR MECHANICS 
690 1 0 |a MYCOBACTERIUM TUBERCULOSIS 
690 1 0 |a NONHUMAN 
690 1 0 |a QUANTUM CHEMISTRY 
690 1 0 |a QUANTUM MECHANICS 
690 1 0 |a REACTION ANALYSIS 
690 1 0 |a SIMULATION 
690 1 0 |a STRESS 
690 1 0 |a ANIONS 
690 1 0 |a BINDING SITES 
690 1 0 |a COMPUTER SIMULATION 
690 1 0 |a HEMOGLOBINS, ABNORMAL 
690 1 0 |a LIGANDS 
690 1 0 |a MODELS, MOLECULAR 
690 1 0 |a MYCOBACTERIUM TUBERCULOSIS 
690 1 0 |a NITRATES 
690 1 0 |a NITRIC OXIDE 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN STRUCTURE, TERTIARY 
690 1 0 |a WATER 
700 1 |a Bidon-Chanal, A. 
700 1 |a Crespo, A. 
700 1 |a Yeh, S.-R. 
700 1 |a Guallar, V. 
700 1 |a Luque, F.J. 
700 1 |a Estrin, D.A. 
773 0 |d 2008  |g v. 130  |h pp. 1688-1693  |k n. 5  |p J. Am. Chem. Soc.  |x 00027863  |w (AR-BaUEN)CENRE-19  |t Journal of the American Chemical Society 
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856 4 0 |u https://doi.org/10.1021/ja076853+  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00027863_v130_n5_p1688_Marti  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v130_n5_p1688_Marti  |y Registro en la Biblioteca Digital 
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