Two light-transducing membrane proteins: bacteriorhodopsin and the mammalian rhodopsin.
- 15 February 1993
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 90 (4) , 1166-1171
- https://doi.org/10.1073/pnas.90.4.1166
Abstract
Site-directed mutagenesis has provided insight into the mechanisms of action oThis publication has 37 references indexed in Scilit:
- Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsin.Journal of Biological Chemistry, 1992
- Bacteriorhodopsin, a membrane protein that uses light to translocate protons.Journal of Biological Chemistry, 1988
- Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation.Proceedings of the National Academy of Sciences, 1987
- Total synthesis of a gene for bovine rhodopsin.Proceedings of the National Academy of Sciences, 1986
- Light-Induced Interaction between Rhodopsin and the GTP-Binding Protein. Metarhodopsin II Is the Major Photoproduct InvolvedEuropean Journal of Biochemistry, 1982
- Bacteriorhodopsin and Related Pigments of HalobacteriaAnnual Review of Biochemistry, 1982
- Bacteriorhodopsin and the purple membrane of halobacteriaBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1979
- Molecular mechanisms for proton transport in membranes.Proceedings of the National Academy of Sciences, 1978
- Three-dimensional model of purple membrane obtained by electron microscopyNature, 1975
- The Molecular Basis of Visual ExcitationNature, 1968