Over-expression of neuroglobin (NGB) in neural tissues of vertebrates promotes cell survival under hypoxic or ischemic conditions. It is postulated that NGB activity could be a part of redox regulated processes in response to hypoxia induced oxidative stress. The human morph of NGB (HNGB) has a disulfide bond switch (residues C46 and C55) positioned on the surface of the protein in the CD loop region. We show that information about cellular redox conditions may be transferred from the surface to the active center involving residue Y44. We postulate a mechanism for redox dependent activation of HNGB through hydrogen bond assisted control of access to the heme-binding site.

Disulfide bond in human neuroglobin determines heme-apoenzyme hydrogen bonding: A possible mechanism for redox control of neuroprotective activity

245th National Meeting (2013)

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