The Binding of Nucleotides to Domain I Proteins of the Proton-Translocating Transhydrogenases from Rhodospirillum rubrum and Escherichia coli as Measured by Equilibrium Dialysis
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1996.0737u.x/fullpdf
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1. Substitution of Tyrosine 146 in the dI Component of Proton-translocating Transhydrogenase Leads to Reversible Dissociation of the Active Dimer into Inactive Monomers;Journal of Biological Chemistry;2007-12
2. 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
3. The Role of Invariant Amino Acid Residues at the Hydride Transfer Site of Proton-translocating Transhydrogenase;Journal of Biological Chemistry;2006-05
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5. Nucleotide binding affinities of the intact proton-translocating transhydrogenase from Escherichia coli;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2005-07
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