1. Charged Amino Acid Substitutions Affect Conformation of Neuroglobin and Cytochrome c Heme Groups
- Author
-
Marina A. Semenova, Zhanna V. Bochkova, Olga M. Smirnova, Georgy V. Maksimov, Mikhail P. Kirpichnikov, Dmitry A. Dolgikh, Nadezda A. Brazhe, and Rita V. Chertkova
- Subjects
neuroprotection ,cytochrome c ,neuroglobin ,heme ,heme proteins ,resonance Raman spectroscopy ,Biology (General) ,QH301-705.5 - Abstract
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.
- Published
- 2024
- Full Text
- View/download PDF