The DCCD-binding polypeptide alone is insufficient for proton translocation through F0 in membranes of Escherichia, coli
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
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2. Membrane Proteins in Energy Transduction;Bragg,1979
3. The Proton-Translocating Pumps of Oxidative Phosphorylation
4. The proteolipid of a mutant ATPase fromEscherichia colidefective in H+-conduction contains a glycine instead of the carbodiimide-reactive aspartyl residue
5. Amino acid replacement in dicyclohexylcarbodiimide-reactive proteins from mutant strains ofescherichia colidefective in the energy- transducing ATPase complex
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1. Anomalous effect of uncouplers on respiratory chain-linked transhydrogenation in Escherichia coli membranes: Evidence for a localized proton pathway?;Archives of Biochemistry and Biophysics;1992-03
2. Topological analysis of the pyridine nucleotide transhydrogenase of Escherichia coli using proteolytic enzymes;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1991-10
3. A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments.;Journal of Biological Chemistry;1990-06
4. BACTERIAL ADENOSINE 5'-TRIPHOSPHATE SYNTHASE (F1F0) - PURIFICATION AND RECONSTITUTION OF F0 COMPLEXES AND BIOCHEMICAL AND FUNCTIONAL-CHARACTERIZATION OF THEIR SUBUNITS;MICROBIOL REV;1987
5. Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits;Microbiological Reviews;1987-12
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