Evidence of .ALPHA.-Helix Slidings during Bacteriorhodopsin Photocycle-Energetics Coupling.
نویسندگان
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 کاملEvidence for a perturbation of arginine-82 in the bacteriorhodopsin photocycle from time-resolved infrared spectra.
Arginine-82 (R82) of bacteriorhodopsin (bR) has long been recognized as an important residue due to its absolute conservation in the archaeal rhodopsins and the effects of R82 mutations on the photocycle and proton release. However, the nature of interactions between R82 and other residues of the protein has remained difficult to decipher. Recent NMR studies showed that the two terminal nitroge...
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 کاملTime-course and stoichiometry of fight-induced proton release and uptake during the photocycle of bacteriorhodopsin
The kinetics and stoi~hiometry of lint-indu~d proton release in purple membrane sus~nsions have been investigated using the pH-indicator dye pyranine and sin~5tu~over flash spectroscopy at a time resolution of 0.1 ps. The number of protons detected by pyranine is inversely proportional to the buffehng power of the medium and 1.1 f 0.2 protons are released per photocycling bacteriorhodopsin mole...
متن کاملChemical and physical evidence for multiple functional steps comprising the M state of the bacteriorhodopsin photocycle.
In the photocycle of bacteriorhodopsin (bR), light-induced transfer of a proton from the Schiff base to an acceptor group located in the extracellular half of the protein, followed by reprotonation from the cytoplasmic side, are key steps in vectorial proton pumping. Between the deprotonation and reprotonation events, bR is in the M state. Diverse experiments undertaken to characterize the M st...
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ژورنال
عنوان ژورنال: The Tohoku Journal of Experimental Medicine
سال: 1997
ISSN: 0040-8727,1349-3329
DOI: 10.1620/tjem.182.15