[HTML][HTML] Human neuroglobin functions as a redox-regulated nitrite reductase
Neuroglobin is a highly conserved hemoprotein of uncertain physiological function that
evolved from a common ancestor to hemoglobin and myoglobin. It possesses a six-
coordinate heme geometry with proximal and distal histidines directly bound to the heme
iron, although coordination of the sixth ligand is reversible. We show that deoxygenated
human neuroglobin reacts with nitrite to form nitric oxide (NO). This reaction is regulated by
redox-sensitive surface thiols, cysteine 55 and 46, which regulate the fraction of the five …
evolved from a common ancestor to hemoglobin and myoglobin. It possesses a six-
coordinate heme geometry with proximal and distal histidines directly bound to the heme
iron, although coordination of the sixth ligand is reversible. We show that deoxygenated
human neuroglobin reacts with nitrite to form nitric oxide (NO). This reaction is regulated by
redox-sensitive surface thiols, cysteine 55 and 46, which regulate the fraction of the five …