|
ИСТИНА |
Войти в систему Регистрация |
ФНКЦ РР |
||
Amino Acid Substitutions in the Non-Ordered Ω-Loop 70–85 Affect Electron Transfer Function and Secondary Structure of Mitochondrial Cytochrome cстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 6 октября 2021 г.
- Авторы: Chertkova Rita V., Bryantseva Tatyana V., Brazhe Nadezhda A., Kudryashova Kseniya S., Revin Victor V., Nekrasov Alexei N., Yusipovich Alexander I., Brazhe Alexey R., Rubin Andrew B., Dolgikh Dmitry A., Kirpichnikov Mikhail P., Maksimov Georgy V.
- Журнал: Crystals
- Том: 11
- Год издания: 2021
- Издательство: MDPI
- Местоположение издательства: Basel, Switzerland
- Первая страница: 973
- Последняя страница: 988
- DOI: 10.3390/cryst11080973
- Аннотация: Abstract: The secondary structure of horse cytochrome c with mutations in the P76GTKMIFA83 site of the Ω-loop, exhibiting reduced efficiency of electron transfer, were studied. CD spectroscopy studies showed that the ordering of mutant structure increases by 3–6% compared to that of the WT moleculesduetothehighercontentof β-structuralelements. TheIRspectroscopydataareconsistent with the CD results and demonstrate that some α-helical elements change into β-structures, and the amount of the non-structured elements is decreased. The analysis of the 1H-NMR spectra demonstrated that cytochrome c mutants have a well-determined secondary structure with some specific features related to changes in the heme microenvironment. The observed changes in the structure of cytochrome c mutants are likely to be responsible for the decrease in the conformational mobility of the P76GTKMIFA83 sequence carrying mutations and for the decline in succinate:cytochrome c-reductase and cytochrome c-oxidase activities in the mitoplast system in the presence of these cytochromes c. We suggest that the decreased efficiency of the electron transfer of the studied cytochromes c may arise due to: (1) the change in the protein conformation in sites responsible for the interaction of cytochrome c with complexes III and IV and (2) the change in the heme conformation thatdeterioratesitsoptimalorientationtowardsdonorandacceptorincomplexesIIIandIVtherefore slowsdownelectrontransfer. Theresultsobtainedareconsistentwiththepreviouslyproposedmodel of mitochondrial cytochrome c functioning associated with the deterministic mobility of protein globule parts.
- Добавил в систему: Максимов Георгий Владимирович