Literature DB >> 17532149

Mycobacterial truncated hemoglobins: from genes to functions.

Paolo Ascenzi1, Martino Bolognesi, Mario Milani, Michel Guertin, Paolo Visca.   

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.

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Year:  2007        PMID: 17532149     DOI: 10.1016/j.gene.2007.02.043

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  16 in total

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6.  Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin.

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7.  Nitric oxide and oxygen regulate truncated hemoglobin gene expression in Frankia strain CcI3.

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Review 9.  Mycobacterial survival strategies in the phagosome: defence against host stresses.

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10.  Covalent attachment of the heme to Synechococcus hemoglobin alters its reactivity toward nitric oxide.

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