Reaction Coupling, Acceptor pK, and Diffusion Control in Light Induced Proton Release of Bacteriorhodopsin
نویسندگان
چکیده
منابع مشابه
Electric-field induced pK-changes in bacteriorhodopsin.
Bacteriorhodopsin, the only protein of the purple membranes of halobacteria [ 11, acts as a light-driven proton pump, translocating protons from the inner to the outer side of the plasma membrane [2]. The lightinduced asymmetric proton distribution contributes to the membrane potential by up to lo-40 mV [3]. Assuming a membrane thickness of 50 A, this potential difference corresponds to an elec...
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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...
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in the area of automotive engineering there is a tendency to more electrification of power train. in this work control of an induction machine for the application of electric vehicle is investigated. through the changing operating point of the machine, adapting the rotor magnetization current seems to be useful to increase the machines efficiency. in the literature there are many approaches wh...
15 صفحه اولMechanism of primary proton transfer in bacteriorhodopsin.
Recent structures of putative intermediates in the bacteriorhodopsin photocycle have provided valuable snapshots of the mechanism by which protons are pumped across the membrane. However, key steps remain highly controversial, particularly the proton transfer occurring immediately after retinal trans-->cis photoisomerization. The gradual release of stored energy is inherently nonequilibrium: wh...
متن کاملpK(a) Calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin.
Calculations of protonation states and pK(a) values for the ionizable groups in the resting state of bacteriorhodopsin have been carried out using the recently available 1.55 A resolution X-ray crystallographic structure. The calculations are in reasonable agreement with the available experimental data for groups on or near the ion transport chain (the retinal Schiff base; Asp85, 96, 115, 212, ...
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ژورنال
عنوان ژورنال: The Journal of Physical Chemistry B
سال: 2002
ISSN: 1520-6106,1520-5207
DOI: 10.1021/jp0261004