The pH dependences of reactions catalyzed by the complete proton-translocating transhydrogenase from Rhodospirillum rubrum, and by the complex formed from its recombinant nucleotide-binding domains
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference40 articles.
1. The proton-translocating nicotinamide adenine dinucleotide transhydrogenase
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3. Molecular biology of nicotinamide nucleotide transhydrogenase — a unique proton pump
4. Estimation of the H+/H− ratio of the reaction catalysed by the nicotinamide nucleotide transhydrogenase in chromatophores from over-expressing strains of Rhodospirillum rubrum and in liposomes inlaid with the purified bovine enzyme
5. Kinetic resolution of the reaction catalysed by proton-translocating transhydrogenase from Escherichia coli as revealed by experiments with analogues of the nucleotide substrates
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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. A review of the binding-change mechanism for proton-translocating transhydrogenase;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2012-10
3. The specificity of proton-translocating transhydrogenase for nicotinamide nucleotides;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2011-01
4. Inhibition of proton-transfer steps in transhydrogenase by transition metal ions;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2009-10
5. Structures of the dI2dIII1 Complex of Proton-Translocating Transhydrogenase with Bound, Inactive Analogues of NADH and NADPH Reveal Active Site Geometries,;Biochemistry;2007-02-27
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