Photothermal Studies with Biological Photoreceptors. The Bacteriorhodopsin Photocycle
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چکیده
منابع مشابه
Protein conformational changes in the bacteriorhodopsin photocycle.
We report a comprehensive electron crystallographic analysis of conformational changes in the photocycle of wild-type bacteriorhodopsin and in a variety of mutant proteins with kinetic defects in the photocycle. Specific intermediates that accumulate in the late stages of the photocycle of wild-type bacteriorhodopsin, the single mutants D38R, D96N, D96G, T46V, L93A and F219L, and the triple mut...
متن کاملA correlation between proton pumping and the bacteriorhodopsin photocycle.
In an attempt to establish a relationship between proton pumping and the photocycle intermediates of bacteriorhodopsin, we have studied the effects of pH and temperature on flash-induced proton pumping and the photointermediates O640 and M412. The relative quantum yield of flash-induced proton pumping is both pH and temperature dependent. It is high in the acid pH range and at low temperatures ...
متن کاملEarly picosecond events in the photocycle of bacteriorhodopsin.
The primary processes of the photochemical cycle of light-adapted bacteriorhodopsin (BR) were studied by various experimental techniques with a time resolution of 5 x 10(-13) s. The following results were obtained. (a) After optical excitation the first excited singlet state S(1) of bacteriorhodopsin is observed via its fluorescence and absorption properties. The population of the excited singl...
متن کامل1 Phenomenological Characterization of Bacteriorhodopsin – D 85 N Photocycle
An operational characterization of the molecular photocycle of a genetic variant of bacteriorhodopsin, BR–D85N, is presented. Steady-state bleach spectra and pump–probe absorbance data are obtained with thick hydrated films containing BR–D85N embedded in a gelatin host. Simple twoand three-state models are used to analyze the photocycle dynamics and extract relevant information such as pure-sta...
متن کاملPHOTOCYCLE AND PROTON TRANSLOCATION IN BACTERIORHODOPSIN Bacteriorhodopsin (bR), a natural photochromic protein from Halobacterium salinarum (formerly H. halo
This review deals with the role of carboxylic amino acids in the proton transport activity of bacteriorhodopsin. The main focus is on the infrared data, which allow direct monitoring of the protonation/deprotonation of specific residues dur ing the proton movement in the course of the photocycle. Additional attention is paid to the potential use of carboxylic acids in proteins as internal senso...
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ژورنال
عنوان ژورنال: Journal Of The Brazilian Chemical Society
سال: 1995
ISSN: 0103-5053
DOI: 10.5935/0103-5053.19950030