Neuroglobin (NGB)

Neuroglobin (NGB) is a monomeric globin protein discovered in 2000, preferentially expressed in the nervous system, including high levels in the retina and optic nerve[1][5]. It is structurally similar to myoglobin and hemoglobin but features a unique six-coordinated heme iron with both proximal and distal histidine ligands[1][5]. Neuroglobin binds biological gases such as oxygen, CO, and NO, and can catalyze the reduction of nitrite to nitric oxide, a process that is regulated by redox-sensitive mechanisms and conformational changes in the heme pocket[2][4]. Proposed biological roles of neuroglobin include neuroprotection against hypoxic and ischemic damage, oxidative stress sensing, reactive oxygen/nitrogen species scavenging, and modulation of cellular respiration through NO production[3][4][5]. Although neuroglobin has been suggested as a therapeutic and neuroprotective target, there are currently no established drugs directly targeting NGB, nor validated biomarkers for therapy monitoring. Elevated or altered neuroglobin expression has been observed in conditions of neurodegenerative disease and ischemic injury, suggesting a role in disease mechanisms and as a candidate therapeutic target[1][3][5].

Other names

NeuroglobinNGBNitrite reductase (neuroglobin)Nitrite reductase, neuroglobin

Nitrite reductase activity (catalyzes reduction of nitrite to nitric oxide); Scavenging of free radicals such as peroxynitrite and reactive oxygen/nitrogen species; Potential inhibition of cellular respiration via NO production and cytochrome c oxidase modulation.