原创力文档role of phee15 gate in ligand entry and nitric oxide detoxification function of mycobacterium tuberculosis truncated hemoglobin nphee15门在配体入口和一氧化氮的解毒功能结核分枝杆菌截断血红蛋白n.pdfVIP
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role of phee15 gate in ligand entry and nitric oxide detoxification function of mycobacterium tuberculosis truncated hemoglobin nphee15门在配体入口和一氧化氮的解毒功能结核分枝杆菌截断血红蛋白n
Role of PheE15 Gate in Ligand Entry and Nitric Oxide
Detoxification Function of Mycobacterium tuberculosis
Truncated Hemoglobin N
1. 2. 1 1 ´3 3
Ana Oliveira , Sandeep Singh , Axel Bidon-Chanal , Flavio Forti , Marcelo A. Martı , Leonardo Boechi ,
3 2 1
Dario A. Estrin , Kanak L. Dikshit *, F. Javier Luque *
1 Department of Physical Chemistry and Institute of Biomedicine (IBUB), Faculty of Pharmacy, University of Barcelona - Recinte Torribera, Santa Coloma de Gramenet,
´ ´ ´ ´ ´ ´ ´
Spain, 2 CSIR-Institute of Microbial Technology, Chandigarh, India, 3 Departamento de Quımica Inorganica, Analıtica y Quımica Fısica/Instituto de Quımica Fısica de los
´
Materiales, Medio Ambiente y Energıa (INQUIMAE), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Abstract
The truncated hemoglobin N, HbN, of Mycobacterium tuberculosis is endowed with a potent nitric oxide dioxygenase (NOD)
activity that allows it to relieve nitrosative stress and enhance in vivo survival of its host. Despite its small size, the protein
matrix of HbN hosts a two-branched tunnel, consisting of orthogonal short and long channels, that connects the heme
active site to the protein surface. A novel dual-path mechanism has been suggested to drive migration of O2 and NO to the
distal heme cavity. While oxygen migrates mainly by the short path, a ligand-induced conformational change regulates
opening of the long tunnel br
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