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S. Takemori, T. King (1964)
RECONSTITUTION OF RESPIRATORY CHAIN ENZYME SYSTEMS. 13. SEQUENTIAL FRAGMENTATION OF SUCCINATE OXIDASE: PREPARATION AND PROPERTIES OF SUCCINATE-CYTOCHROME C REDUCTASE AND THE CYTOCHROME B-C1 PARTICLE.The Journal of biological chemistry, 239
O. Lowry, N. Rosebrough, A. Farr, R. Randall (1951)
Protein measurement with the Folin phenol reagent.The Journal of biological chemistry, 193 1
M. Boll (2004)
Studies with Triton X-100 treated electron transport particles from Rhodospirillum rubrumArchiv für Mikrobiologie, 71
K. Davis, Y. Hatefi (1969)
Kinetics of the resolution of complex I (reduced diphosphopyridine nucleotide-coenzyme Q reductase) of the mitochondrial electron transport system by chaotropic agents.Biochemistry, 8 8
M. Boll (2004)
The effect of deoxycholate on enzymes with electron transport function from Rhodospirillum rubrumArchiv für Mikrobiologie, 68
David Green, Alexander Tzagoloff (1966)
The mitochondrial electron transfer chain.Archives of biochemistry and biophysics, 116 1
M. Boll (1970)
Action of sodium dodecyl sulfate on electron transport enzymes ofRhodospirillum rubrumExperientia, 26
R. Eisenberg, L. Yu, M. Wolin (1970)
Divalent Cation Activation of Deoxycholate-Solubilized and -Inactivated Membrane Reduced Nicotinamide Adenine Dinucleotide Oxidase of Bacillus megaterium KMJournal of Bacteriology, 102
Y. Hatefi, Haavik Ag, D. Griffiths (1962)
Studies on the electron transfer system. XL. Preparation and properties of mitochondrial DPNH-coenzyme Q reductase.The Journal of biological chemistry, 237
D. Ziegler, K. Doeg (1962)
Studies on the electron transport system. XLIII. The isolation of a succinic-coenzyme Q reductase from beef heart mitochondriaArchives of Biochemistry and Biophysics, 97
M. Boll (2004)
Enzyme der Elektronentransportpartikel aus Rhodospirillum rubrum: Eigenschaften von NADH- und Succinat-Cytochrom c-ReduktaseArchiv für Mikrobiologie, 64
D. Horgan, Thomas Singer, J. Casida (1968)
Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. 13. Binding sites of rotenone, piericidin A, and amytal in the respiratory chain.The Journal of biological chemistry, 243 4
Y. Hatefi, A. Haavik, L. Fowler, D. Griffiths (1962)
Studies on the electron transfer system. XLII. Reconstitution of the electron transfer system.The Journal of biological chemistry, 237
Studies on the electron transfer chain . XL . Preparation and properties of mitochondrial coenzyme Q - reductase
Y. Hatefi, K. Stempel (1967)
Resolution of complex I (DPNH-coenzyme Q reductase) of the mitochondrial electron transfer system.Biochemical and biophysical research communications, 26 3
F. Crane, C. Widmer, R. Lester, Y. Hatefi, W. Fechner (1959)
Studies on the electron transport system: XV. Coenzyme Q (Q275) and the succinoxidase activity of the electron transport particleBiochimica et Biophysica Acta, 31
J. Rieske (1967)
[44] Preparation and properties of reduced coenzyme Q-cytochrome c reductase (complex III of the respiratory chain)Methods in Enzymology, 10
M. Boll (1970)
Effect of proteolytic and lipolytic Enzymes on the Electron Transport Particle Fraction of Rhodospirillum rubrumZeitschrift für Naturforschung B, 26
M. Boll (2004)
Oxidation of reduced nicotinamide-adenine-dinucleotide in Rhodospirillum rubrumArchiv für Mikrobiologie, 69
S. Razin, Z. Ne'eman, I. Ohad (1969)
Selective reaggregation of solubilized Mycoplasma-membrane proteins and the kinetics of membrane reformation.Biochimica et biophysica acta, 193 2
M. Boll (1968)
Oxydation von reduziertem Nicotinamid-Adenin-Dinucleotid in Rhodospirillum rubrumArchiv für Mikrobiologie, 62
D. Ziegler, J. Rieske (1967)
[42] Preparation and properties of succinate dehydrogenase-coenzyme Q reductase (complex II)Methods in Enzymology, 10
L. Yu, M. Wolin (1970)
Factors Affecting Deoxycholate Inactivation and Mg++ Reactivation of Bacillus megaterium KM Membrane Nicotinamide Adenine Dinucleotide (Reduced Form) OxidaseJournal of Bacteriology, 103
203 76 76 2 2 M. Boll Lehrstuhl für Mikrobiologie Institut für Biologie II der Universität Freiburg i. Br. Freiburg i. Br Germany Summary A comparison between the effects of diethylether and urea on the electron transport system of R. rubrum was made. 1. Both reagents cause an increasing and complete inactivation of NADH oxidation with oxygen and cytochrome c as electron acceptors. The flavoprotein NADH dehydrogenase is only slightly affected. The oxidation of succinate (cytochrome c as electron acceptor) is inactivated only by much higher concentrations of either agent, succinate dehydrogenase being completely unaffected. Low concentrations of urea, in contrast to diethylether, stimulate succinate-cytochrome creductase. A preferential attack of both agents on the NADH → ubiquinone segment is suggested. 2. By treatment of the membranes with diethylether NADH dehydrogenase is transformed to a second, less active state. This form of the enzyme is characterized by a slower V max , a slightly increased k m (NADH), and an unchanged k m (electron acceptor). It cannot be reactivated. 3. Urea, like phosphate, causes a conformational change at the active site of succinate dehydrogenase as evidenced from an identical activation behaviour. 4. About 20% of the particulate activity of NADH dehydrogenase can be released from the membranes by treatment with urea. This activity apparently is identical with that solubilized by deoxycholate.
Archives of Microbiology – Springer Journals
Published: Jun 1, 1971
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