Article
Uncoupling in secondary transport proteins. A mechanistic explanation for mutants of lac permease with an uncoupled phenotype.
The Journal of biological chemistry - 26 May 1995
Lolkema J S, Poolman B
Abstract excerpt
The kinetic behavior of a H(+)-substrate symporter has been studied in which in addition to the unloaded (E) and fully loaded states (E.S.H) of the carrier also one of the binary complexes (E.S or E.H) may reorient its binding sites. This results in two types of uncoupled mutants, the ES leak and...
Topics
- Biological Transport
- Cell Membrane Permeability
- Energy Metabolism
- Escherichia coli Proteins
- Hydrogen-Ion Concentration
- Kinetics
- Lactose
- Membrane Potentials
- Membrane Transport Proteins
- Models, Chemical
- Monosaccharide Transport Proteins
- Mutation
- Phenotype
- Protons
- Symporters