Ascenzi Paolo, Bolognesi Martino, Milani Mario, Guertin Michel, Visca Paolo
National Institute for Infectious Diseases I.R.C.C.S. Lazzaro Spallanzani, Via Portuense 292, I-00149 Roma, Italy.
Gene. 2007 Aug 15;398(1-2):42-51. doi: 10.1016/j.gene.2007.02.043. Epub 2007 Apr 29.
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.
由分枝杆菌属细菌引起的感染是对人类健康最具挑战性的威胁之一。分枝杆菌在活性氮和氧存在的情况下在体内持续存在的能力意味着这些细菌中存在有效的解毒机制。分枝杆菌截短血红蛋白（trHb）最近被认为与活性氮的清除有关。每个trHb家族（N、O和P）的个别成员可能存在于同一分枝杆菌物种中。分枝杆菌trHb的血红素活性位点结构的独特特征，结合不同的配体结合特性和体内表达模式，表明这些球蛋白可能具有多种功能。在此，综述了关于分枝杆菌trHb的最新基因组、结构和生化信息，旨在进一步深入了解这些球蛋白在分枝杆菌生理学中的作用。
