Neuroglobin (Ngb), an enzyme that promotes the survival of neurons under hypoxic conditions, functions via a redox-regulated process according to in vitro and in vivo assays.  We propose a mechanism for the redox control of human Ngb (hNgb) via the influence of the CD loop on the active site, on the basis of X-ray crystal structures and MD simulations.  Our work provides evidence that when the external environment becomes sufficiently oxidizing, the CD loop undergoes a strand-to-helix transition, which causes critical restructuring of the active site. According to our postulate, the strand-to-helix mechanics of the CD loop, enabled by the lability of Cys46/Cys55 disulfide bonding and of the Tyr44/His64/heme propionate interaction network, underlies the redox-controlled functioning of hNgb.

Possible mechanism for redox control of human neuroglobin activity revealed by crystallography and simulation

249th National Meeting (2015)

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