Dae Jong Jang

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The rates of the quenching and recovery of tryptophan fluorescence are determined in the microsecond-millisecond time scale during the photocycle of bacteriorhodopsin under different perturbations. The kinetics suggest the presence of two quenching processes, a rapid one (on the time scale of photocycle intermediate L550 formation or faster) and a slow one(More)
The retinylidene chromophore mutant (Y185F) of bacteriorhodopsin, in which Tyr-185 is substituted by phenylalanine, is examined and compared with wild-type bacteriorhodopsin expressed in Escherichia coli; both were reinstituted similarly in vesicles. The Y185F mutant shows (at least) two distinct spectra at neutral pH. Upon light absorption, the blue(More)
The removal of 75% of the lipid from bacteriorhodopsin caused the following: (i) decreased efficiency and rate of deprotonation of the protonated Schiff base (as monitored by absorption of the M412 intermediate); (ii) increased efficiency of deprotonation of deionized samples; (iii) a decrease by 1 unit in the pH at which deprotonation ceases; (iv)(More)
The transient absorption at 296 nm was part of the spectroscopic evidence that initiated the proposal that tyrosinate (Tyr-) is formed during, and important to, the photocycle of bacteriorhodopsin (bR). Recent evidence against such a proposal comes from the results of NMR, UV Raman as well as electron cryo-microscopic structural studies. This makes it(More)
Introduction There has been lower the tilt margin by the increase of coma aberration due to the reduction of wavelength and the increase of numerical aperture for high density recording. The RF signal degradation is increased as the decrease of tilt margin. To compensate the tilt margjn, the optical pick-up actuator for high-speed CD/DVD re -writable system(More)
Intramolecular electron transfer in partially reduced cytochrome c oxidase has been studied by the perturbed equilibrium method. We have prepared a three-electron-reduced, CO-inhibited form of the enzyme in which cytochrome a and copper A are partially reduced and in an intramolecular redox equilibrium. When these samples were irradiated with a nitrogen(More)
In this work we study the decay of the polarization of the Trp fluorescence in native bacteriorhodopsin (bR), deionized bR (dlbR), and the retinal-free form of bR, bacterioopsin (bO), using picosecond laser/streak camera system. Two types of depolarization processes are observed, one around 250 ps, which is temperature independent around room temperature,(More)
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