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Mycobacterial truncated hemoglobins: From genes to functions

Academic Article
Publication Date:
2007
abstract:
Infections caused by bacteria belonging to genus Mycobacterium are among the most challenging threats for human health. The ability of mycobacteria to persist in vivo in the presence of reactive nitrogen and oxygen species implies the presence in these bacteria of effective detoxification mechanisms. Mycobacterial truncated hemoglobins (trHbs) have recently been implicated in scavenging of reactive nitrogen species. Individual members from each trHb family (N, O, and P) can be present in the same mycobacterial species. The distinct features of the heme active site structure combined with different ligand binding properties and in vivo expression patterns of mycobacterial trHbs suggest that these globins may accomplish diverse functions. Here, recent genomic, structural and biochemical information on mycobacterial trHbs is reviewed, with the aim of providing further insights into the role of these globins in mycobacterial physiology. (c) 2007 Elsevier B.V. All rights reserved.
Iris type:
01.01 Articolo in rivista
Keywords:
PEROXYNITRITE-MEDIATED OXIDATION; HYDROGEN-BOND NETWORK; NITRIC-OXIDE; TUBERCULOSIS HEMOGLOBIN; REACTIVE NITROGEN
List of contributors:
Bolognesi, Martino; MILANI DE MAYO DE MARI, Mario
Authors of the University:
MILANI DE MAYO DE MARI MARIO
Handle:
https://iris.cnr.it/handle/20.500.14243/123286
Published in:
GENE
Journal
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