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- W2083416621 abstract "Neuroglobin (Ngb) is a hexacoordinate globin expressed in the nervous system of vertebrates, involved in neuroprotection. O2 equilibrium measurements on mouse Ngb yielded significantly different P50 values, ranging from ∼2 torr to ∼10 torr. By a kinetic approach minimizing the effects of protein autoxidation, we measured P50 = 2.2 torr at 20 °C. As predicted from the structure, O2 binds to the Y44D Ngb mutant more quickly (k = 2.2 s−1 vs 0.15 s−1) and with slightly higher affinity (P50 = 1.3 torr) than wild-type. In addition, we introduced a novel reduction protocol for metNgb based on NADH:flavorubredoxin oxidoreductase (FlRd-red) from Escherichia coli, a candidate for the Ngb reducing activity recently identified in E. coli extracts. Interestingly, E. coli FlRd-red shares sequence similarity with the FAD-binding domain of the human apoptosis-inducing factor, a finding which may have unexpected significance with reference to the mechanism of neuroprotection by Ngb." @default.
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- W2083416621 date "2008-03-01" @default.
- W2083416621 modified "2023-10-12" @default.
- W2083416621 title "Neuroglobin: Enzymatic reduction and oxygen affinity" @default.
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- W2083416621 doi "https://doi.org/10.1016/j.bbrc.2008.01.021" @default.
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