Histidine 225, a Residue of the NhaA-Na+/H+ Antiporter of Escherichia coli Is Exposed and Faces the Cell Exterior
Open Access
- 1 January 1997
- journal article
- Published by Elsevier
- Vol. 272 (3), 1761-1768
- https://doi.org/10.1074/jbc.272.3.1761
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Probing the Conformation of the Lactose Permease ofEscherichia colibyin SituSite-Directed Sulfhydryl ModificationBiochemistry, 1996
- Replacements of Histidine 226 of NhaA-Na+/H+ Antiporter of Escherichia coliJournal of Biological Chemistry, 1995
- Dynamics of Lactose Permease of Escherichia coli Determined by Site-Directed Chemical Labeling and Fluorescence SpectroscopyBiochemistry, 1995
- Molecular physiology of Na+/H+ antiporters, key transporters in circulation of Na+ and H+ in cellsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1994
- Transmembrane Protein Structure: Spin Labeling of Bacteriorhodopsin MutantsScience, 1990
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989
- Electrochemical proton gradient in inverted membrane vesicles from Escherichia coliBiochemistry, 1980
- Sodium-proton antiport in isolated membrane vesicles of Escherichia coliBiochemistry, 1978
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Direct determination of ΔpH in chloroplasts, and its relation to the mechanisms of photoinduced reactionsFEBS Letters, 1971