Document Detail

Photocycle in the M-form in bacteriorhodopsin mutants devoid of primary proton acceptor Asp-85.
MedLine Citation:
PMID:  11817568     Owner:  NLM     Status:  MEDLINE    
Photoinduced changes in absorption of the deprotonated M-form in the mutant bacteriorhodopsin without primary proton acceptor Asp-85 were studied and additional evidence in support of the complete transmembrane proton transfer in photocycle was obtained. Measurements of the absorption spectrum were carried out at various pH, temperature, and humidity. The direction of proton transfer was the same as in the normal photocycle of the wild-type bacteriorhodopsin: from the internal to the external side of the membrane. The effect on this process of a terminal acceptor Glu-204 was shown.
E P Lukashev; P Kolodner
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Membrane & cell biology     Volume:  14     ISSN:  1023-6597     ISO Abbreviation:  Membr Cell Biol     Publication Date:  2001  
Date Detail:
Created Date:  2002-01-30     Completed Date:  2002-06-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9517472     Medline TA:  Membr Cell Biol     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  715-25     Citation Subset:  IM    
Biophysical Department, Biological Faculty, Lomonosov Moscow State University, Russia.
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MeSH Terms
Aspartic Acid / chemistry*
Bacteriorhodopsins / chemistry*,  genetics
Halobacterium salinarum
Hydrogen-Ion Concentration
Spectrum Analysis
Reg. No./Substance:
0/Protons; 53026-44-1/Bacteriorhodopsins; 56-84-8/Aspartic Acid

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