Evidence for substrate-induced conformational changes in mitochondrial transhydrogenase
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(75)80494-7/fullpdf
Reference20 articles.
1. Factors Governing the Kinetics and Steady State of the Mitochondrial Nicotinamide Nucleotide Transhydrogenase System
2. Steady-State Kinetics of Mitochondrial Nicotinamide Nucleotide Transhydrogenase. 2. The Energy-Linked Reaction
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1. 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
2. Energy-transducing nicotinamide nucleotide transhydrogenase. Nucleotide binding properties of the purified enzyme and proteolytic fragments.;Journal of Biological Chemistry;1993-08
3. Chapter 11 The energy-transducing nicotinamide nucleotide transhydrogenase;Molecular Mechanisms in Bioenergetics;1992
4. The proton-translocating nicotinamide adenine dinucleotide transhydrogenase;Journal of Bioenergetics and Biomembranes;1991-10
5. Mitochondrial energy-linked nicotinamide nucleotide transhydrogenase: effect of substrates on the sensitivity of the enzyme to trypsin and identification of tryptic cleavage sites;Biochemistry;1990-05-01
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