Mutation of Conserved Polar Residues in the Transmembrane Domain of the Proton-Pumping Pyridine Nucleotide Transhydrogenase ofEscherichia coli
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference34 articles.
1. A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change
2. The involvement of NADP(H) binding and release in energy transduction by proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli
3. Mechanism of hydride transfer during the reduction of 3-acetylpyridine adenine dinucleotide by NADH catalyzed by the pyridine nucleotide transhydrogenase ofEscherichia coli
4. Mutation of Conserved Residues in the NADP(H)-Binding Domain of the Proton Translocating Pyridine Nucleotide Transhydrogenase ofEscherichia coli
5. Cloning and expression of the transhydrogenase gene of Escherichia coli
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1. Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel;FEBS Letters;2015-07-02
2. Proton-Translocating Transhydrogenase in Photosynthetic Bacteria;The Purple Phototrophic Bacteria;2009
3. Molecular Recognition between Protein and Nicotinamide Dinucleotide in Intact, Proton-Translocating Transhydrogenase Studied by ATR-FTIR Spectroscopy;Journal of the American Chemical Society;2006-02-04
4. Nucleotide binding affinities of the intact proton-translocating transhydrogenase from Escherichia coli;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2005-07
5. Zinc ions selectively inhibit steps associated with binding and release of NADP(H) during turnover of proton-translocating transhydrogenase;FEBS Letters;2005-04-27
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