Temperature dependence of protein fluorescence in Rb. sphaeroides reaction centers frozen to 80 K in the dark or on the actinic light as the indicator of protein conformational dynamics.
Dokl Biochem Biophys
; 467(1): 105-9, 2016 Mar.
Article
em En
| MEDLINE
| ID: mdl-27193710
ABSTRACT
The differences in the average fluorescence lifetime (τav) of tryptophanyls in photosynthetic reaction center (RC) of the purple bacteria Rb. sphaeroides frozen to 80 K in the dark or on the actinic light was found. This difference disappeared during subsequent heating at the temperatures above 250 K. The computer-based calculation of vibration spectra of the tryptophan molecule was performed. As a result, the normal vibrational modes associated with deformational vibrations of the aromatic ring of the tryptophan molecule were found. These deformational vibrations may be active during the nonradiative transition of the molecule from the excited to the ground state. We assume that the differences in τav may be associated with the change in the activity of these vibration modes due to local variations in the microenvironment of tryptophanyls during the light activation.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Temperatura
/
Proteínas de Bactérias
/
Rhodobacter sphaeroides
/
Complexo de Proteínas do Centro de Reação Fotossintética
/
Fluorescência
Idioma:
En
Revista:
Dokl Biochem Biophys
Assunto da revista:
BIOFISICA
/
BIOQUIMICA
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Federação Russa