Expression and purification of a novel flavohemoblobin from Mycobaterium tuberculosis

PICCINNI, F.E. BONAMORE A., MARTI M. A., NADRA A.D., BOFFI, A. AND ESTRIN, DARÍO A

Congreso; XLII Reunión annual de la Sociedad Argentina de Biofísica; 2013

Flavohemoglobins, widely found in bacteria and yeast, have both a globin and a ferrodoxin reductase domain (FAD-bindingdomain). The flavohemoglobin from E. coli has been thoroughly characterized as an important feature against nitrosative stress. A novelflavohemoglobin studied in M. tuberculosis shows some structural similarity to the latter one from E. coli. However, it is thought to havea different role in protection against oxidative damage that does not include NO scavenging. The cell membrane is protected by itscycling between the ferrous and ferric state due to a D-lactate dehydrogenase activity.