| Literature DB >> 7578054 |
G Váró1, L S Brown, J Sasaki, H Kandori, A Maeda, R Needleman, J K Lanyi.
Abstract
The photochemical cycle of the light-driven chloride pump, halorhodopsin from N. pharaonis, is described by transient optical multichannel and single-wavelength spectroscopy in the visible, and in the infrared. Titration of a blue-shift of the absorption maximum upon addition of chloride describes a binding site with a KD of 1 mM. The reaction sequence after the all-trans to 13-cis photoisomerization of the retinal in this chloride binding form is itself dependent on chloride. At 2 M chloride it is described by the scheme: HR-->K<==>L<==>N-->HR that relaxes in a few milliseconds, and is very similar to the photocycle of bacteriorhodopsin under conditions where the retinal Schiff base cannot deprotonate. At lower chloride concentrations, e.g., 0.1 M, however, a red-shifted state termed O appears between N and HR, in equilibrium with N. The absorption spectra of K, L, N, and O are very similar to their counterparts in the bacteriorhodopsin photocycle. As in their equivalents in bacteriorhodopsin, in the N state the retinal is still 13-cis, but it is reisomerized in the O state to all-trans.Entities:
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Year: 1995 PMID: 7578054 DOI: 10.1021/bi00044a027
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162