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NADH Dehydrogenases: From Basic Science to Biomedicine

Journal of Bioenergetics and Biomembranes, 2001
This review article is concerned with two on-going research projects in our laboratory, both of which are related to the study of the NADH dehydrogenase enzyme complexes in the respiratory chain. The goal of the first project is to decipher the structure and mechanism of action of the proton-translocating NADH-quinone oxidoreductase (NDH-1) from two ...
T, Yagi   +5 more
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The NADH Dehydrogenase of the Respiratory Chain

1970
The long recognized importance of the NADH dehydrogenase of the respiratory chain in linking the oxidation of most of the metabolically generated NADH to the terminal electron transport system and the complex and unusual properties of this flavoprotein probably account for the wide-spread interest which has been focused on this enzyme during the past ...
Thomas P. Singer, M. Gutman
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The transformation of mitochondrial NADH dehydrogenase into NADH: Cytochrome c oxidoreductase

Biochimica et Biophysica Acta, 1963
Abstract 1. 1. Depending on the temperature of digestion of the Keilin and Hartree heartmuscle preparation with snake-venom phospholipase, two different soluble preparations catalysing the oxidation of NADH can be obtained. 2. 2. Digestion at 30° yields a preparation with acceptor specificity, inhibitor sensitivity and stability resembling ...
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Stoichiometry of the nadh-oxidoreductase reaction for dehydrogenase determinations

Clinica Chimica Acta, 1980
The NADH oxidoreductase reaction with resazurin was most rapid at pH 6.5. FMN (10 mumol/l) markedly stimulated the reaction, and the optimal concentration of resazurin was 50 mumol/l. The oxidation of NADH by NADH oxidoreductase with resaruzin as electron acceptor gave a variable yield of fluorescent product, resorufin.
S, Barnes, J G, Spenney
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A simple method for the purification of the mitochondrial NADH dehydrogenase

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1971
Abstract A simple procedure for the isolation and purification of the high-molecular-weight type NADH dehydrogenase from beef heart mitochondria is reported.
P C, Huang, R L, Pharo
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Reduction of 2-pyridinecarboxaldehyde by a dehydrogenase-NADH model

Bioorganic Chemistry, 1988
Abstract Zinc 1-(α-2-methyl-1,10-phenanthroline)-1,4-dihydronicotinamide has been synthetized as a model for the enzyme-coenzyme complex of NADH-alcohol dehydrogenase. The model forms with 2-pyridinecarboxaldehyde a ternary complex in which the phenanthroline-bound zinc ion activates the aldehyde group for reduction.
Engbersen, J.F.J.   +2 more
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Fuscin, an Inhibitor of NADH Dehydrogenase

1969
I wish to say a few words about a respiratory inhibitor named Fuscin which blocks the transfer of electrons in the respiratory chain at the level of the first site as rotenone and amytal do [1, 2]. I also take this opportunity to express my thanks to Professor D. H. R.
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Reconstitutively active NADH dehydrogenase

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1969
S P, Albracht, E C, Slater
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NADH dehydrogenase

1994
D. Schomburg, M. Salzmann, D. Stephan
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