Exploring the nitric oxide detoxification mechanism of mycobacterium tuberculosis truncated haemoglobin N
Mycobacterium tuberculosis, the causative agent of human tuberculosis, encodes a haemoprotein named Truncated Haemoglobin N (trHbN), which in its active site transforms nitric oxide (NO) to nitrate anion. (NO3 -). The NO-dioxygenase activity of trHbN seems to be crucial for the bacillus, which can s...
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2009
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| 003 | AR-BaUEN | ||
| 005 | 20230518203828.0 | ||
| 008 | 190411s2009 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-67649746267 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 100 | 1 | |a Bidon-Chanal, A. | |
| 245 | 1 | 0 | |a Exploring the nitric oxide detoxification mechanism of mycobacterium tuberculosis truncated haemoglobin N |
| 260 | |c 2009 | ||
| 270 | 1 | 0 | |m Bidon-Chanal, A.; Departament de Fisicoquímica, Institut de Biomedicina (IBUB), Universitat de Barcelona, AV. Diagonal 643, 08028 Barcelona, Spain; email: fjluque@ub.edu |
| 506 | |2 openaire |e Política editorial | ||
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| 504 | |a Pawaria, S., Rajamohan, G., Gambhir, V., Lama, A., Varshney, G.C., Dikshit, K.L., Intracellular growth and survival of Salmonella enterica serovar Typhimurium carrying truncated hemoglobins of Mycobacterium tuberculosis (2007) Microb Pathog, 42, pp. 119-128 | ||
| 504 | |a Milani, M., Pesce, A., Ouellet, Y., Ascenzi, P., Guertin, M., Bolognesi, M., Mycobacterium tuberculosis hemoglobin N displays a protein tunnel for O2 diffusion to the heme (2001) EMBO J, 20, pp. 3902-3909 | ||
| 504 | |a Springer, B.A., Egeberg, K.D., Sligar, S.G., Rohlfs, R.J., Mathews, A.J., Olson, J.S., Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Sitedirected mutagenesis of the distal histidine (1989) J Biol Chem, 264, pp. 3057-3060 | ||
| 504 | |a Eich, R.F., Li, T., Lemon, D.D., Doherty, D.H., Curry, S.R., Aitken, J.F., Mathews, A.J., Olson, J.S., Mechanism of NO-induced oxidation of myoglobin and hemoglobin (1996) Biochemistry-US, 35, pp. 6976-6983 | ||
| 504 | |a Bidon-Chanal, A., Martí, M.A., Crespo, A., Milani, M., Orozco, M., Bolognesi, M., Luque, F.J., Estrin, D.A., Ligand-induced dynamical regulation of NO conversion in Mycobacterium tuberculosis truncated hemoglobin-N (2006) Proteins, 64, pp. 457-464 | ||
| 504 | |a Ouellet, Y., Milani, M., Couture, M., Bolognesi, M., Guertin, M., Ligand interactions in the distal heme pocket of Mycobacterium tuberculosis truncated hemoglobin N: Roles of TyrB10 and GlnE11 residues (2006) Biochemistry-US 2006, 45, pp. 8770-8781 | ||
| 504 | |a Bidon-Chanal, A., Martí, M.A., Estrin, D.A., Luque, F.J., Dynamical regulation of ligand migration by a gate-opening molecular switch in truncated hemoglobin-N from Mycobacterium tuberculosis (2007) J Am Chem Soc, 129, pp. 6782-6788 | ||
| 504 | |a Crespo, A., Martí, M.A., Kalko, S.G., Morreale, A., Orozco, M., Gelpi, J.L., Luque, F.J., Estrin, D.A., Theoretical study of the truncated hemoglobin HbN: Exploring the molecular basis of the NO detoxification mechanism (2005) J Am Chem Soc, 127, pp. 4433-4444 | ||
| 504 | |a Martí, M.A., Bidon-Chanal, A., Crespo, A., Yeh, S.R., Guallar, V., Luque, F.J., Estrin, D.A., Mechanism of product release in NO detoxification from Mycobacterium tuberculosis truncated hemoglobin N (2008) J Am Chem Soc, 130, pp. 1688-1693 | ||
| 520 | 3 | |a Mycobacterium tuberculosis, the causative agent of human tuberculosis, encodes a haemoprotein named Truncated Haemoglobin N (trHbN), which in its active site transforms nitric oxide (NO) to nitrate anion. (NO3 -). The NO-dioxygenase activity of trHbN seems to be crucial for the bacillus, which can survive under the nitrosative stress conditions that occur upon infection of the host. As a defense mechanism against the copious amounts of NO produced by macrophages upon infection, the protein must achieve a high level of NO-dioxygenase activity to eliminate NO, but this is modulated by its efficiency in capturing O2 and NO. Migration of small diatomic ligands through the protein matrix is related to the presence of a doubly branched tunnel system connecting the surface and the haem cavity site. In this work, we have studied the mechanism that controls ligand diffusion and product egression with state-of-the-art molecular dynamics simulations. The results support a dual path mechanism for migration of O2 and NO through distinct branches of the tunnel, where migration of NO is facilitated upon binding of O2 to the haem group. Finally, egression of (NO3 -) is preceded by the entrance of water to the haem cavity and occurs through a different pathway. Overall, the results highlight the intimate relationship between structure, dynamical behavior and biological function of trHbN. © 2009 Springer Science + Business Media B.V. |l eng | |
| 593 | |a Departament de Fisicoquímica, Institut de Biomedicina (IBUB), Universitat de Barcelona, AV. Diagonal 643, 08028 Barcelona, Spain | ||
| 593 | |a Departamento de Química Inorgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón II, Buenos Aires (C1428EHA), Argentina | ||
| 690 | 1 | 0 | |a LIGAND MIGRATION |
| 690 | 1 | 0 | |a MOLECULAR SIMULATIONS |
| 690 | 1 | 0 | |a MYCOBACTERIUM TUBERCULOSIS |
| 690 | 1 | 0 | |a NO DETOXIFICATION |
| 690 | 1 | 0 | |a TRUNCATED HAEMOGLOBIN N |
| 690 | 1 | 0 | |a MYCOBACTERIUM TUBERCULOSIS |
| 700 | 1 | |a Martí, M.A. | |
| 700 | 1 | |a Estrín, D.A. | |
| 700 | 1 | |a Luque, F.J. | |
| 773 | 0 | |d 2009 |h pp. 33-47 |p NATO Sci. Peace Secur. Ser. A Chem. Biol. |x 18746489 |z 9789048124831 |t NATO Science for Peace and Security Series A: Chemistry and Biology | |
| 856 | 4 | 1 | |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-67649746267&doi=10.1007%2f978-90-481-2590-6_3&partnerID=40&md5=f12431d31c7f82a5defd5c1b149965aa |y Registro en Scopus |
| 856 | 4 | 0 | |u https://doi.org/10.1007/978-90-481-2590-6_3 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_18746489_v_n_p33_BidonChanal |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_18746489_v_n_p33_BidonChanal |y Registro en la Biblioteca Digital |
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