4 results match your criteria: "Biological Faculty of the M.V. Lomonosov Moscow State University[Affiliation]"
Comparison of tryptophan fluorescence lifetimes in cyanobacterial photosystem I frozen in the light and in the dark.
Photosynth Res
March 2019
Department of Biophysics, Biological Faculty of the M.V. Lomonosov Moscow State University, Moscow, Russia, 119991.
Article Synopsis
- The study investigates the effects of temperature on tryptophan fluorescence lifetime in trimeric photosystem I (PSI) complexes from cyanobacteria at varying temperatures from -180 °C to 20 °C.
- Samples frozen in light exhibited longer fluorescence lifetimes compared to those frozen in the dark, with specific lifetimes noted for components within 65% glycerol.
- The analysis highlighted how temperature variations influence protein dynamics and electron transfer in cyanobacterial PSI compared to Rhodobacter sphaeroides complexes, revealing an antiphase relationship between certain fluorescence components' contributions.
Hybrid complexes of photosynthetic reaction centers and quantum dots in various matrices: resistance to UV irradiation and heating.
Photosynth Res
March 2019
Department of Biophysics, Biological Faculty of the M.V. Lomonosov Moscow State University, Moscow, Russia, 119991.
The effects of ultraviolet (UV) irradiation (up to 0.6 J/cm) and heating (65 °C, 20 min) on the absorption spectra and electron transfer in dehydrated film samples of photosynthetic reaction centers (RCs) from purple bacterium Rhodobacter (Rb.) sphaeroides, as well as in hybrid structures consisting of RCs and quantum dots (QDs), have been studied.
View Article and Find Full Text PDFThe effect of light and temperature on the dynamic state of Rhodobacter sphaeroides reaction centers proteins determined from changes in tryptophan fluorescence lifetime and PQ recombination kinetics.
J Photochem Photobiol B
March 2018
Department of Biophysics, Biological Faculty of the M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
Article Synopsis
- The study explored how temperature impacts the rate of dark recombination between charges in photosynthetic reaction centers of Rhodobacter sphaeroides.
- Measurements were taken in water-glycerol and trehalose environments at extremely low temperatures, assessing both the recombination rates and fluorescence lifetimes of tryptophan.
- Findings indicate two main microconformations in the reaction centers, suggesting different electron transfer dynamics based on whether the centers were frozen in the dark or under light.
Photosystem 2 effective fluorescence cross-section of cyanobacterium Synechocystis sp. PCC6803 and its mutants.
J Photochem Photobiol B
September 2011
Department of Biophysics, Biological Faculty of the M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
The effective fluorescence cross-section of photosystem 2 (PS2) was defined by measurements of chlorophyll a fluorescence induction curves for the wild type of the unicellular cyanobacterium Synechocystis sp. PCC6803, C-phycocyanin deficient mutant (CK), and mutant that totally lacks phycobilisomes (PAL). It was shown that mutations lead to a strong decrease of the PS2 effective fluorescence cross-section.
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