|
ИСТИНА |
Войти в систему Регистрация |
ИПМех РАН |
||
The influence of chemical chaperones on electron stabilization processes in the photosynthetic reaction centers of Rb.sphaeroidesтезисы доклада
- Авторы: Knox P.P., Seifullina N.Kh
- Сборник: Book of abstracts of Second international conference “Nanobiophysics 201: Fundamental and applied aspects”, Kiev, oct.2011, p. 115
- Тезисы
- Год издания: 2011
- Место издания: Kiev
- Первая страница: 115
- Аннотация: The molecular dynamics of proteins is influenced by their interactions with chemical chaperones (CCs), i.e., low molecular weight compounds that are capable of correcting the structural-dynamic state of proteins, including those responsible for the development of a number of health problems. Well characterized CCs include alkylated hydroxybenzenes (AHBs), which can enhance the functional and operational stability of a number of enzyme proteins. The goal of this work was to investigate the effect of AHBs on the operation of the RCs of purple bacteria and assess the possible application of RCs for the purpose of selecting the biologically active substances influencing the the structural-dynamic state of functional proteins. The following AHB were used as structural modifiers of the RC protein: 5n-methylresorcinol (5MR),4n-hexylresorcinol (4HR),2-(4-hydroxyphenyl)ethanol (tyrosol, T), 2n-methylresorcinol (2MR), 5n-ethylresorcinol (5ER). The influence of structurally different AHBs on the temporary stabilization of the electron on the primary quinone acceptor of RCs was investigated. The addition of all tested AHB to RC preparation resulted in an increase in characteristic time of the P+–QA- recombination rate. The extent of the effect depended on both the AHB concentration and structure. It increased in the sequence T, 2MR, 5MR, 5ER, 4HR, which correlated with the hydrophobicity degree of these AHB. The increase in characteristic time of P+-QA- recombination may be due to the functioning of the alkyl radicals in the AHBs’ aromatic nucleus and their hydroxyl groups. The hydroxyl groups obviously exert an influence on the RC system of hydrogen bonds the state of which affects the functional activity of the RCs. This is consistent with the higher efficiency of 5MR compared to 2MR, the alkyl radical of which screens the hydroxyl groups. However, the manifest dependence of the modifying effect of exogenous substances on the hydrophobicity of their molecules suggests a decisive role of hydrophobic interactions between AHB and the RC protein. The results indicate that the RC can be used as a convenient model system for the primary testing of biologically active substances for the porpose of assessing their potential employment as efficient modifiers of the functional activities of biopolymers.
- Добавил в систему: Нокс Петр Петрович