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SHR Neuro Krebs Kardio Lipid Stoffw Microb

Magyari, K; Bálint, Z; Simon, V; Váró, G.
The photochemical reaction cycle of retinal reconstituted bacteriorhodopsin.
J Photochem Photobiol B. 2006; 85(2):140-144 Doi: 10.1016/j.jphotobiol.2006.05.009
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Co-Autor*innen der Med Uni Graz
Balint Zoltan
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Abstract:
The function of three types of bacteriorhodopsins was compared: the wild-type, the bleached and retinal reconstituted and retinal deficient bacteriorhodopsin after retinal addition. The apparent pK(a) of the proton acceptor group for the bleached BR and retinal deficient BR shifted toward higher pH values compared to the wild-type BR. Fitting the photocycle model to the absorption kinetic signals for all three proteins showed the existence of the same intermediates, but the time-dependent concentration of the intermediates was different. Although measurements were made at pH 7, the absorption kinetics and photoelectric signals in both retinal reconstituted samples acted as wild-type bacteriorhodopsin at significantly higher pH. Below pH 3 the retinal deficient and reconstituted sample bleached. These results suggested that the added retinal was not able to rebind in the same position in the protein as in native bacteriorhodopsin. This points out that care should be taken, when bleached bacteriorhodopsin is reconstituted with different retinal analogs.
Find related publications in this database (using NLM MeSH Indexing)
Bacteriorhodopsins - chemistry Bacteriorhodopsins - metabolism
Halobacterium salinarum - chemistry Halobacterium salinarum - metabolism
Hydrogen-Ion Concentration -
Kinetics -
Photochemistry -
Retinaldehyde - chemistry
Spectrum Analysis -
Titrimetry -

Find related publications in this database (Keywords)
retinal protein
photocycle
absorption kinetics
retinal reconstitution
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