Insights into heme degradation and hydrogen peroxide-induced dimerization of human neuroglobin.

ABSTRACT: In this present study, we investigated the H2O2-induced oligomerization of wild-type human neuroglobin (hNgb) and of some selected variants (C46AC55A, Y44A, Y44F, Y44AC46AC55A, Y44AC46AC55A) to clarify how the process is affected by the Cys46/Cys55 disulfide bond and the distal H-bonding network and to figure out the molecular determinants of the H2O2-induced formation of amyloid-type structures and hNgb aggregates. It turns out that hydrogen peroxide exerts a two-fold effect on hNgb, inducing both heme breakdown and protein dimerization/polymerization. The enhanced resistance to the oxidizing effect of H2O2 of the disulfide-free variants indicates that both effects are strictly influenced by the heme accessibility for H2O2. Most importantly, the H2O2-induced neuroglobin dimerization/polym

SUBMITTER: Cassiani A 

PROVIDER: S-EPMC12096953 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature