Главная Назад


Авторизация
Идентификатор пользователя / читателя
Пароль (для удалённых пользователей)
 

Вид поиска

Область поиска
Найдено в других БД
Формат представления найденных документов:
библиографическое описаниекраткийполный
Поисковый запрос: (<.>S=СПЕКТРОСКОПИЯ РАМАНОВСКАЯ РЕЗОНАНСНАЯ<.>)
Общее количество найденных документов : 1
1.
РЖ ВИНИТИ 34 (BI16) 96.02-04В3.18

   

    Surface-enhanced resonance Raman scattering spectroscopy of photosystem II pigment-protein complexes [Text] / Rafael Picorel [et al.] // J. Phys. Chem. - 1994. - Vol. 98, N 23. - P6017-6022 . - ISSN 0022-3654
Перевод заглавия: Исследование комплекса пигмент-белок фотосистемы II методом резонансной рамановской спектроскопии с поверхностным усилением
Аннотация: Three different photosystem II (PSII) pigment-protein complexes (D1-D2-Cyt b[559]-CP47, D1-D2-Cyt b[559], and CP47) isolated from spinach were studied by surface-enhanced resonance Raman scattering (SERRS) spectroscopy. Surface-enhanced Raman scattering (SERS) is a distance sensitive (on a 5-10-A scale) spectroscopic tool that can be used to examine structural properties of large biological molecules. It is demonstrated here that SERS can also be used to determine organizational relationships between different pigment-protein complexes. Strong SERRS spectra from the above PSII complexes before and after treatment with sodium dithionite were obrained on roughened Ag electrodes and in citrate-reduced Ag colloids. The D1-D2-Cyt b[559] complex adsorbs with the Cyt b[559] heme close to the surface in the colloid, whereas the complex adsorbs differently on the Ag electrode due to the differing surface properties of the two types of substrates. An analysis of the SERRS spectra led to the following conclusions: CP47 binds next to Cyt b[559] in the D1-D2-Cy b[559] - CP47 complex and covers the heme, the Cyt b[559] heme is located closer to one side of the complex (the stromal side in the intact thylakoid membrane), and both Chl and 'бета'-carotene molecules are located closer to the opposite side of the complex. Assuming a barrel-shape structure for the pigment-protein complexes, the results imply that the complexes are oriented with the central axis perpendicular to the metal surface both in the colloids and on the electrodes. США, Photoconversion Branch, Natl. Renewable Energy Lab., 1617 Cole Blvd., Golden, Colorado 80401. Библ. 37
ГРНТИ  
ВИНИТИ 341.31.17.25
Рубрики: ФОТОСИСТЕМА II
КОМПЛЕКС ПИГМЕНТ-БЕЛОК

СПЕКТРОСКОПИЯ РАМАНОВСКАЯ РЕЗОНАНСНАЯ


Доп.точки доступа:
Picorel, Rafael; Chumanov, George; Cotton, Therese M.; Montoya, Guillermo; Toon, Stephen; Seibert, Michael


 




© Международная Ассоциация пользователей и разработчиков электронных библиотек и новых информационных технологий
(Ассоциация ЭБНИТ)