A catalytically active complex formed from the recombinant dI protein of Rhodospirillum rubrum transhydrogenase, and the recombinant dIII protein of the human enzyme
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference31 articles.
1. 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
2. Interdomain hydride transfer in proton-translocating transhydrogenase
3. Domains, specific residues and conformational states involved in hydride ion transfer and proton pumping by nicotinamide nucleotide transhydrogenase from Escherichia coli
4. Site-directed mutagenesis of the proton-pumping pyridine nucleotide transhydrogenase of Escherichia coli
5. Physiological roles of nicotinamide nucleotide transhydrogenase
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1. Proton-Translocating Nicotinamide Nucleotide Transhydrogenase: A Structural Perspective;Frontiers in Physiology;2017-12-19
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. Proton-Translocating Transhydrogenase in Photosynthetic Bacteria;The Purple Phototrophic Bacteria;2009
5. A hybrid of the transhydrogenases from Rhodospirillum rubrum and Mycobacterium tuberculosis catalyses rapid hydride transfer but not the complete, proton-translocating reaction;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2006-03
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