Interactions of reduced and oxidized nicotinamide mononucleotide with wild-type and αD195E mutant proton-pumping nicotinamide nucleotide transhydrogenases from Escherichia coli-Reference-Cited by-同舟云学术

Interactions of reduced and oxidized nicotinamide mononucleotide with wild-type and αD195E mutant proton-pumping nicotinamide nucleotide transhydrogenases from Escherichia coli

Published:1998-10 Issue:1-3 Volume:1367 Page:134-138
ISSN:0005-2728
Container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics

Author:

Hu Xiang,Zhang Junwei,Rydström Jan

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference20 articles.

1. The proton-translocating nicotinamide adenine dinucleotide transhydrogenase

2. Molecular biology of nicotinamide nucleotide transhydrogenase — a unique proton pump

3. Nicotinamide nucleotide transhydrogenase: a model for utilization of substrate binding energy for proton translocation

4. Conformational Dynamics of a Mobile Loop in the NAD(H)-Binding Subunit of Proton-Translocating Transhydrogenases from Rhodospirillum Rubrum and Escherichia Coli

5. Structural and Catalytic Properties of the Expressed and Purified NAD(H)- and NADP(H)-Binding Domains of Proton-Pumping Transhydrogenase from Escherichia coli

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Interactions of the NADP(H)-Binding Domain III of Proton-Translocating Transhydrogenase from Escherichia coli with NADP(H) and the NAD(H)-Binding Domain I Studied by NMR and Site-Directed Mutagenesis;Biochemistry;2000-09-23

2. Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties11This review is dedicated to the memory of Professor Lars Ernster.;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-04