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    
Abstract/OtherAbstract:
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.
Authors:
E P Lukashev; P Kolodner
Related Documents :
1113138 - Electron microscopy of trypsin-digested peripheral nerve myelin.
3427038 - Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 1. m412 ...
7213618 - Lipid--protein interactions in bacteriorhodopsin--dimyristoylphosphatidylcholine vesicles.
21058698 - Effect of lipid phase transition on molecular assembly and structural stability of bact...
24007978 - Lipids of mitochondria.
11015918 - Thermal unbinding of highly oriented phospholipid membranes.
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    
Affiliation:
Biophysical Department, Biological Faculty, Lomonosov Moscow State University, Russia. lukashev@biophys.msu.ru
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Aspartic Acid / chemistry*
Bacteriorhodopsins / chemistry*,  genetics
Halobacterium salinarum
Hydrogen-Ion Concentration
Kinetics
Mutation
Photochemistry
Protons
Spectrum Analysis
Temperature
Chemical
Reg. No./Substance:
0/Protons; 53026-44-1/Bacteriorhodopsins; 56-84-8/Aspartic Acid

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Pathways of the abscisic acid hormonal signal transduction across the plant cell plasma membrane.
Next Document:  Transcription factors NF-kappaB and AP-1/c-fos in cell response to nocodazole.