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PMID: 1526960 Published · ppublish English Journal Article Review

A unifying concept for ion translocation by retinal proteins.

Journal of bioenergetics and biomembranes ·Vol. 24 ·No. 2 ·1992-04-00 ·Pages 181-91

Oesterhelt D, Tittor J, Bamberg E

Abstract

First, halorhodopsin is capable of pumping protons after illumination with green and blue light in the same direction as chloride. Second, mutated bacteriorhodopsin where the proton acceptor Asp85 and the proton donor Asp96 are replaced by Asn showed proton pump activity after illumination with blue light in the same direction as wildtype after green light illumination. These results can be explained by and are discussed in light of our new hypothesis: structural changes in either molecule lead to a change in ion affinity and accessibility for determining the vectoriality of the transport through the two proteins.

MeSH Terms
Amino Acid Sequence Bacteriorhodopsins/chemistry,metabolism Biological Transport Halorhodopsins Ions Models, Biological Molecular Sequence Data
Chemicals
Halorhodopsins Ions Bacteriorhodopsins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Oesterhelt D
Max-Planck-Institu für Biochemie, Martinsried, Germany.
Tittor J
Bamberg E
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Article Info
Journal
Journal of bioenergetics and biomembranes
Abbr.
J Bioenerg Biomembr
ISSN
0145-479X
DOI
10.1007/BF00762676
Published
1992-04-00
Pages
181-91
Language
English
Region
United States
NLM ID
7701859
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00762676 View journal details
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