Document Detail


Substitution of amino acids in helix F of bacteriorhodopsin: effects on the photochemical cycle.
MedLine Citation:
PMID:  2575916     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The effects of amino acid substitutions in helix F of bacteriorhodopsin on the photocycle of this light-driven proton pump were studied. The photocycles of Ser-183----Ala and Glu-194----Gln mutants were qualitatively similar to that of wild-type bacteriorhodopsin produced in Escherichia coli and bacteriorhodopsin from Halobacterium halobium. The substitution of a Phe for either Trp-182 or Trp-189 significantly reduced the fraction of photocycling bacteriorhodopsin. The amino acid substitutions Tyr-185----Phe and Ser-193----Ala substantially increased the lifetime of the photocycle without substantially increasing the lifetime of the M photocycle intermediate. Similar results were also obtained with the Pro-186----Gly substitution. In contrast, replacing Pro-186 with the larger residue Leu inhibited the formation of the M photocycle intermediate. These results are consistent with a structural model of the retinal-binding pocket suggested by low-temperature UV/visible and Fourier transform infrared difference spectroscopies that has Trp-182, Tyr-185, Pro-186, and Trp-189 forming part of the binding pocket.
Authors:
P L Ahl; L J Stern; T Mogi; H G Khorana; K J Rothschild
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  28     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1989 Dec 
Date Detail:
Created Date:  1990-03-27     Completed Date:  1990-03-27     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  10028-34     Citation Subset:  IM    
Affiliation:
Department of Physics, Boston University, Massachusetts 02215.
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MeSH Terms
Descriptor/Qualifier:
Alanine
Amino Acid Sequence
Amino Acids / metabolism*
Bacteriorhodopsins / metabolism*
Glutamates
Glutamic Acid
Glutamine
Glycine
Hydrogen Bonding
Kinetics
Leucine
Molecular Sequence Data
Mutation
Phenylalanine
Photochemistry
Proline
Protons
Serine
Tryptophan
Grant Support
ID/Acronym/Agency:
AI-11479/AI/NIAID NIH HHS; GM28289-06/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Glutamates; 0/Protons; 147-85-3/Proline; 53026-44-1/Bacteriorhodopsins; 56-40-6/Glycine; 56-41-7/Alanine; 56-45-1/Serine; 56-85-9/Glutamine; 56-86-0/Glutamic Acid; 61-90-5/Leucine; 63-91-2/Phenylalanine; 73-22-3/Tryptophan

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


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