BACK, NATHAN, COHEN, IRUN R., KRITCHEVSKY, DAVID, LAJTHA, ABEL, PAOLETTI, RODOLFO, Hayashida, Yoshiaki, Gonzalez, Constancio, Kondo, Hisatake, DI GIULIO, C., BIANCHI, G., CACCHIO, M., ARTESE, L., PICCIRILLI, M., VERRATTI, V., VALERIO, R., and ITURRIAGA, R.
Neuroglobin (Ngb), a 151-amino-acid protein with a predicted molecular mass of 17 kD was recently identified as a member of the vertebrate globin family (Burmester and Hankeln, 2004; Mammen et al., 2002). Ngb, is predominantly expressed in nerve cells, particularly in the brain and in the retina (Burmester et al., 2000; Zhu et al., 2002), but is also expressed in other tissues (Burmester and Hankeln, 2004). The protein has three-on-three -helical globin fold and are endowed with a hexa-coordinate heme-Fe atoms, which displays O2 affinities and binds CO (Burmester & Hankeln, 2004).The physiological role of Ngb is not well understood, but it has been proposed that Ngb participates in several processes such as oxygen transport, oxygen storage, and NO detoxification (Burmester and Hankeln, 2004). Ngb as well as hemoglobin is a respiratory protein that reversibly binds gaseous ligands (NO and O2) by means of the Fe-containing porphyrin ring. Ngb is concentrated in neuronal cellular regions that contain mitochondria, and its distribution is correlated with oxygen consumption rates (Pesce et al., 2003). [ABSTRACT FROM AUTHOR]