Many pathogenic microorganisms have evolved hemoglobin-mediated nitric oxide (NO)
detoxification mechanisms, where a globin domain in conjunction with a partner reductase …

Mycobacterium tuberculosis truncated hemoglobin, HbN, is endowed with a potent nitric-
oxide dioxygenase activity and has been found to relieve nitrosative stress and enhance in …

The survival of Mycobacterium tuberculosis requires detoxification of host· NO. Oxygenated
Mycobacterium tuberculosis truncated hemoglobin N catalyzes the rapid oxidation of nitric …

The previously reported nitric oxide precursor [Mn (PaPy2Q) NO] ClO4 (1), where
(PaPy2QH) is N, N-bis (2-pyridylmethyl)-amine-N-ethyl-2-quinoline-2-carboxamide, was …

The potent nitric oxide dioxygenase (NOD) activity (trHbN–Fe2+–O2+• NO→ trHbN–Fe3+–
OH2+ NO3–) of Mycobacterium tuberculosis truncated hemoglobin N (trHbN) protects …

Mycobacterium tuberculosis, the causative agent of human tuberculosis, is forced into
latency by nitric oxide produced by macrophages during infection. In response to nitrosative …

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 …

Nitric oxide (NO), generated in large amounts within the macrophages, controls and restricts
the growth of internalized human pathogen, Mycobacterium tuberculosis H37Rv. The …

FeBMbs are structural and functional models of native bacterial nitric oxide reductases
(NORs) generated through engineering of myoglobin. These biosynthetic models replicate …

The capability of Mycobacterium tuberculosis to rest in latency in the infected organism
appears to be related to the disposal of detoxification mechanisms, which converts the nitric …