Article
The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85.
Biochemistry - 11 Oct 1994
Brown L S, Gat Y, Sheves M, Yamazaki Y, Maeda A, Needleman R, Lanyi J K
Abstract excerpt
Bacteriorhodopsin contains all-trans-retinal linked via a protonated Schiff base to K216. The proton transport in this pump is initiated by all-trans to 13-cis photoisomerization of the retinal and the ensuing transfer of the Schiff base proton to D85. Changed geometrical relationship of the Schi...
Topics
- Aspartic Acid
- Bacteriorhodopsins
- Biological Transport
- Halobacterium salinarum
- Hydrogen-Ion Concentration
- Linear Models
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Photoperiod
- Photosynthetic Reaction Center Complex Proteins
- Proton Pumps
- Recombinant Proteins
