Ligand-induced dynamical regulation of NO conversion in Mycobacterium tuberculosis truncated hemoglobin-N
Mycobacterium tuberculosis, the causative agent of human tuberculosis, is forced into latency by nitric oxide produced by macrophages during infection. In response to nitrosative stress M. tuberculosis has evolved a defense mechanism that relies on the oxygenated form of "truncated hemoglobin&q...
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| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
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Wiley-Liss Inc.
2006
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 11491caa a22012257a 4500 | ||
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| 001 | PAPER-7065 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203648.0 | ||
| 008 | 190411s2006 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-33745593982 | |
| 024 | 7 | |2 cas |a dioxygenase, 37292-90-3; heme, 14875-96-8; hemoglobin, 9008-02-0; nitrate, 14797-55-8; nitric oxide, 10102-43-9; oxygen, 7782-44-7 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a PSFGE | ||
| 100 | 1 | |a Bidon-Chanal, A. | |
| 245 | 1 | 0 | |a Ligand-induced dynamical regulation of NO conversion in Mycobacterium tuberculosis truncated hemoglobin-N |
| 260 | |b Wiley-Liss Inc. |c 2006 | ||
| 270 | 1 | 0 | |m Luque, F.J.; University of Barcelona, Av. Diagonal 643, 08028, Barcelona, Spain; email: fjluque@ub.edu |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a Mycobacterium tuberculosis, the causative agent of human tuberculosis, is forced into latency by nitric oxide produced by macrophages during infection. In response to nitrosative stress M. tuberculosis has evolved a defense mechanism that relies on the oxygenated form of "truncated hemoglobin" N (trHbN), formally acting as NO-dioxygenase, yielding the harmless nitrate ion. X-ray crystal structures have shown that trHbN hosts a two-branched protein matrix tunnel system, proposed to control diatomic ligand migration to the heme, as the rate-limiting step in NO conversion to nitrate. Extended molecular dynamics simulations (0.1 μs), employed here to characterize the factors controlling diatomic ligand diffusion through the apolar tunnel system, suggest that O2 migration in deoxy-trHbN is restricted to a short branch of the tunnel, and that O2 binding to the heme drives conformational and dynamical fluctuations promoting NO migration through the long tunnel branch. The simulation results suggest that trHbN has evolved a dual-path mechanism for migration of O2 and NO to the heme, to achieve the most efficient NO detoxification. © 2006 Wiley-Liss, Inc. |l eng | |
| 593 | |a Departament de Fisicoquímica, Facultat de Farmacia, Universität de Barcelona, Av. Diagonal 643, 08028, Barcelona, Spain | ||
| 593 | |a Departamento de Quimica Inorganica, Analitica y Quimica Fisica/INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EHA, Argentina | ||
| 593 | |a Department of Biomolecular Sciences and Biotechnology, CNR-INFM, University of Milano, Milano, Italy | ||
| 593 | |a Departament de Bioquímica i Biologia Molecular, Facultat de Química, Universitat de Barcelona, Martí i Franqués 1, 08028 Barcelona, Spain | ||
| 593 | |a Unidad de Modelización Molecular y Bioinformática, Parc Científic de Barcelona, Josep Samitier 1-6, 08028 Barcelona, Spain | ||
| 593 | |a Span and Computacional Biology Program, Barcelona Supercomputing Center, Edificio Nexus II, Barcelona 08028, Spain | ||
| 593 | |a University of Buenos Aires, Department of Chemistry, Ciudad Universitaria, Buenos Aires, C1428EHA, Argentina | ||
| 593 | |a University of Barcelona, Av. Diagonal 643, 08028, Barcelona, Spain | ||
| 690 | 1 | 0 | |a LIGAND MIGRATION |
| 690 | 1 | 0 | |a M. TUBERCULOSIS |
| 690 | 1 | 0 | |a MOLECULAR DYNAMICS |
| 690 | 1 | 0 | |a NITRIC OXIDE |
| 690 | 1 | 0 | |a DEOXY TRUNCATED HEMOGLOBIN N |
| 690 | 1 | 0 | |a DIOXYGENASE |
| 690 | 1 | 0 | |a HEME |
| 690 | 1 | 0 | |a HEMOGLOBIN |
| 690 | 1 | 0 | |a LIGAND |
| 690 | 1 | 0 | |a NITRATE |
| 690 | 1 | 0 | |a NITRIC OXIDE |
| 690 | 1 | 0 | |a OXYGEN |
| 690 | 1 | 0 | |a TRUNCATED HEMOGLOBIN N |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a BIOINFORMATICS |
| 690 | 1 | 0 | |a CONFORMATIONAL TRANSITION |
| 690 | 1 | 0 | |a CRYSTAL STRUCTURE |
| 690 | 1 | 0 | |a DEFENSE MECHANISM |
| 690 | 1 | 0 | |a DIFFUSION |
| 690 | 1 | 0 | |a LATENT PERIOD |
| 690 | 1 | 0 | |a MACROPHAGE |
| 690 | 1 | 0 | |a MOLECULAR DYNAMICS |
| 690 | 1 | 0 | |a MYCOBACTERIUM TUBERCULOSIS |
| 690 | 1 | 0 | |a NITROSATION |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a OXYGEN AFFINITY |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN CONFORMATION |
| 690 | 1 | 0 | |a PROTEIN FUNCTION |
| 690 | 1 | 0 | |a SIMULATION |
| 690 | 1 | 0 | |a STRUCTURE ANALYSIS |
| 690 | 1 | 0 | |a X RAY CRYSTALLOGRAPHY |
| 690 | 1 | 0 | |a MYCOBACTERIUM TUBERCULOSIS |
| 700 | 1 | |a Martí, M.A. | |
| 700 | 1 | |a Crespo, A. | |
| 700 | 1 | |a Milani, M. | |
| 700 | 1 | |a Orozco, M. | |
| 700 | 1 | |a Bolognesi, M. | |
| 700 | 1 | |a Luque, F.J. | |
| 700 | 1 | |a Estrin, D.A. | |
| 773 | 0 | |d Wiley-Liss Inc., 2006 |g v. 64 |h pp. 457-464 |k n. 2 |p Proteins Struct. Funct. Genet. |x 08873585 |t Proteins: Structure, Function and Genetics | |
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