Results 291 to 300 of about 465,834 (342)

The external NADH dehydrogenases of intact plant mitochondria

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
Abstract Evidence is given for the presence of two NADH dehydrogenase systems accessible to exogenous NADH in mitochondria from mung bean hypocotyls. One system, which is located on the outer membrane, contains a flavoprotein and cytochrome b555, is insensitive to antimycin A and is specific for the 4α hydrogen atom of NADH.
R, Douce, C A, Mannella, W D, Bonner
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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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EPR behavior of a soluble cardiac NADH dehydrogenase

Biochemical and Biophysical Research Communications, 1973
Abstract A soluble, lipid free, NADH dehydrogenase isolated from cardiac muscle shows the characteristic iron-sulfide centers similar to those found in submitochondrial particles and mitochondria. The g -values obtained by low temperature EPR spectroscopy are 2.026, 1.943 and 1.927 for temperature “insensitive” center 1; 2.058 and 1.943 for ...
D, DerVartanian, R F, Baugh, T E, King
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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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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., Koudijs, A., van der Plas, H.C.   +2 more
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Photophysical processes in the NADH—alcohol dehydrogenase complex

Journal of Photochemistry and Photobiology B: Biology, 1992
Fluorescent analysis showed the high sensitivity of the NADH-alcohol dehydrogenase complex to UV irradiation. The complex reacts to UV illumination with "photoresponse," a rapid decrease in NADH fluorescence intensity to some stationary level. No such decrease was found in the NADH solution without the protein.
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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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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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