Charged Amino Acid Substitutions Affect Conformation of Neuroglobin and Cytochrome c Heme Groups

Charged Amino Acid Substitutions Affect Conformation of Neuroglobin and Cytochrome c Heme Groups

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Neuroglobin (Ngb) is a cytosolic heme protein that plays an important role in protecting cells from apoptosis through interaction with oxidized cytochrome c (Cyt c) released from mitochondria.The interaction of reduced Ngb and oxidized Cyt c is accompanied by electron transfer between them and the reduction in Cyt c.Despite the growing number Wooden Train Set of studies on Ngb, the mechanism of interaction between Ngb and Cyt c is still unclear.

Using Raman spectroscopy, we studied the effect of charged amino acid Soft Doll substitutions in Ngb and Cyt c on the conformation of their hemes.It has been shown that Ngb mutants E60K, K67E, K95E and E60K/E87K demonstrate changed heme conformations with the lower probability of the heme planar conformation compared to wild-type Ngb.Moreover, oxidized Cyt c mutants K25E, K72E and K25E/K72E demonstrate the decrease in the probability of methyl-radicals vibrations, indicating the higher rigidity of the protein microenvironment.

It is possible that these changes can affect electron transfer between Ngb and Cyt c.