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Primary light-energy conversion in tetrameric chlorophyll structure of photosystem II and bacterial reaction centers: II. Femto- and picosecond charge separation in PSII D1/D2/Cyt b559 complex.
Photosynth Res
March 2009
NN Semenov Institute of Chemical Physics, Russian Academy of Sciences, 117991 Moscow, Russia.
In Part I of the article, a review of recent data on electron-transfer reactions in photosystem II (PSII) and bacterial reaction center (RC) has been presented. In Part II, transient absorption difference spectroscopy with 20-fs resolution was applied to study the primary charge separation in PSII RC (DI/DII/Cyt b 559 complex) excited at 700 nm at 278 K. It was shown that the initial electron-transfer reaction occurs within 0.
View Article and Find Full Text PDFComparative study of spectral flexibilities of bacterial light-harvesting complexes: structural implications.
Biophys J
April 2006
Department of Biophysics and Physics of Complex Systems, Division of Physics and Astronomy, Faculty of Sciences, Vrije Universiteit, 1081 HV Amsterdam, The Netherlands.
This work presents a comparative study of the frequencies of spectral jumping of individual light-harvesting complexes of six different types: LH2 of Rhodopseudomonas acidophila, Rhodobacter sphaeroides, and Rhodospirillum molischianum; LH1 of Rhodobacter sphaeroides; and two "domain swap mutants" of LH2 of Rhodobacter sphaeroides: PACLH1 and PACLH2mol, in which the alpha-polypeptide C-terminus is exchanged with the corresponding sequence from LH1 of Rhodobacter sphaeroides or LH2 of Rhodospirillum molischianum, respectively. The quasistable states of fluorescence peak wavelength that were previously observed for the LH2 of Rps. acidophila were confirmed for other species.
View Article and Find Full Text PDFProtonation, photobleaching, and photoactivation of yellow fluorescent protein (YFP 10C): a unifying mechanism.
Biochemistry
April 2005
Department of Chemistry, Stanford University, CA 94305, USA.
Yellow fluorescent protein (YFP 10C) is widely used as a probe in biology, but its complex photochemistry gives rise to unusual behavior that requires fuller definition. Here we characterize the kinetics of protonation and reversible bleaching over time scales of picoseconds to hours. Stopped-flow and pressure-jump techniques showed that protonation of the fluorescent YFP(-) anion state is two-step with a slow transition that accounts for blinking of 527 nm emission at the single molecule level on the seconds time scale.
View Article and Find Full Text PDFSelective fluorescence recovery after bleaching of single E2GFP proteins induced by two-photon excitation.
Chemphyschem
February 2005
INFM and Department of Physics, University of Milano Bicocca, Piazza della Scienza 3, 20126 Milano, Italy.
We report the two-photon excitation and emission or a recently developed green fluorescent protein (GFP) mutant, E(2)GFP. Two main excitation bands are found at 780 and 870 nm. Blinking and irreversible and reversible bleaching were observed.
View Article and Find Full Text PDFCharacterization of a D1-D2-cyt b-559 complex containing 4 chlorophyll a/2 pheophytin a isolated with the use of MgSO4.
FEBS Lett
February 1994
Max-Planck Institut für Strahlenchemie, Mülheim an der Ruhr, Germany.
A D1-D2-cyt b-559 complex containing 4 chlorophyll alpha, 1 beta-carotene and 1 cytochrome b-559 per 2 pheophytin a has been isolated from spinach with 30% yield using a Q-Sepharose Fast-Flow anion-exchange column equilibrated with 0.1% Triton X-100, 10 mM MgSO4 and 50 mM Tris-HCl (pH 7.2).
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