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

Semenova, M.A.; Bochkova, Z.V.; Smirnova, O.M.; Maksimov, G.V.; Kirpichnikov, M.P.; Dolgikh, D.A.; Brazhe, N.A.; Chertkova, R.V.

Авторы: Semenova Marina A., Bochkova Zhanna V., Smirnova Olga M., Maksimov Georgy V., Kirpichnikov Mikhail P., Dolgikh Dmitry A., Brazhe Nadezda A., Chertkova Rita V.
Журнал: Current Issues in Molecular Biology
Том: 46
Номер: 4
Год издания: 2024
Издательство: Caister Academic Press
Местоположение издательства: United Kingdom
Первая страница: 3364
Последняя страница: 3378
DOI: 10.3390/cimb46040211
Аннотация: 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 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 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.
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Charged Amino Acid Substitutions Affect Conformation of Neuroglobin and Cytochrome c Heme Groupsстатья

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