Results 251 to 260 of about 158,607 (300)

NADH dehydrogenase and NADH oxidation inBacillus megaterium

Current Microbiology, 1986
Only one type (membrane-bound form) of NADH dehydrogenase could be detected in the log-phase cells ofBacillus megaterium. By sonification this enzyme could be effectively solubilized, while NADH oxidase remained bound to the membrane. A molecular weight of about 40 Kd was estimated for the dehydrogenase by gel electrophoresis in the presence of sodium ...
Sambasivamoorthy Thiagalingam, Tsanyen Yang   +1 more
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Mechanism of NADH transfer among dehydrogenases

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998
Steady-state and transient-state kinetic experiments have been performed to test the proposal that there is a direct (channelled) transfer of NADH from one dehydrogenase to another if the two enzymes exhibit distinct chiral coenzyme specificity (A-side vs. B-side).
W M, Arias, H, Pettersson, G, Pettersson
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Terpenylnaphthoquinones are reductively activated by NADH/NADH dehydrogenase

Toxicological & Environmental Chemistry, 2005
Novel terpenylnaphthoquinones were found to enhance the rate of oxygen consumption in the presence of NADH/NADH dehydrogenase in 1 : 1 v/v mixtures of 40 mM phosphate buffer (pH 7.4) and DMSO. Initial rates of oxygen consumption increase with an increase in the half-wave reduction potentials of the quinones.
Antonio E. Alegria, Sheila Sanchez, Pedro Sanchez-Cruz, Ileana Nieves, Nadya G. Cruz, Marina Gordaliza, Maria Luz Martín-Martín   +6 more
openaire   +1 more source

NADH dehydrogenase activity of higher plant nitrate reductase (NADH)

Plant Science Letters, 1979
Abstract Squash nitrate reductase (NADH) was purified on blue-Sepharose and used to study the NADH dehydrogenase activity. In the presence of nitrate reductase. NADH will reduce: nitrate, ferricyanide, methylene blue, benzoquinone and menadione. Coenzyme Q10 and plastiquinone were not reduced.
John Smarrelli, Wilbur H. Campbell
openaire   +1 more source

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, B B, Seo, S, Di Bernardo, E, Nakamaru-Ogiso, M C, Kao, A, Matsuno-Yagi   +5 more
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Thienylvinylindoles as inhibitors of mitochondrial NADH dehydrogenase

Pharmaceutica Acta Helvetiae, 1994
In connection with a previous study, new phenylindoles bearing a 2- or 3-thienyl group were synthesized and tested as specific inhibitors of mitochondrial NADH dehydrogenase. The position of the phenyl ring and the geometrical configuration play an important role in the activity and specificity of these derivatives.
A, Andreani, M, Rambaldi, A, Locatelli, A, Leoni, A, Ghelli, M, Degli Esposti   +5 more
openaire   +2 more sources

Interaction of rhodanese with mitochondrial NADH dehydrogenase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
NADH dehydrogenase is an iron-sulfur flavoprotein which is isolated and purified from Complex I (mitochondrial NADH: ubiquinone oxidoreductase) by resolution with NaClO4. The activity of the enzyme (followed as NADH: 2-methylnaphthoquinone oxidoreductase) increases linearly with protein concentration (in the range between 0.2 and 1.0 mg/ml) and ...
S, Pagani, Y M, Galante
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NADH-linked fumarate reductase and NADH dehydrogenase activities inFibrobacter succinogenes

Current Microbiology, 1994
Crude membrane preparation fromFibrobacter succinogenes S85 were investigated and found to contain NADH dehydrogenase (NADH:decylubiquinone oxidoreductase) and NADH-linked fumarate reductase activities. Under aerobic conditions the maximum NADH dehydrogenase activity (252 nmoles/min/mg protein) was ten times greater than that of NADH-fumarate reductase
Steven W. Meinhardt, Thomas L. Glass
openaire   +1 more source

The Three Families of Respiratory NADH Dehydrogenases

2007
Most reducing equivalents extracted from foodstuffs during oxidative metabolism are fed into the respiratory chains of aerobic bacteria and mitochondria by NADH:quinone oxidoreductases. Three families of enzymes can perform this task and differ remarkably in their complexity and role in energy conversion.
Stefan, Kerscher, Stefan, Dröse, Volker, Zickermann, Ulrich, Brandt   +3 more
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The [4B-3H] NADH-H2O exchange reaction of the mitochondrial NADH dehydrogenase

Biochemical and Biophysical Research Communications, 1985
The purified mitochondrial NADH dehydrogenase enzyme has been shown to catalyze a rapid [4B-3H] NADH-H2O exchange reaction. When the enzyme is subjected to a single freeze-thaw cycle there is a complete loss of NADH dehydrogenation without a measurable decrease in the [4B-3H] NADH-H2O exchange.
S, Chen, R J, Guillory
openaire   +2 more sources