Terminal Oxidations in Bacillus brevis. Soluble Reduced Nicotinamide Adenine Dinucleotide Oxidase Activity in Bacillus brevis

The application of a recently published technique to localize reduced nicotinamide adenine dinucleotide oxidase activity is described in glutaraldehyde-fixed Candida albicans. The reaction product appears as a finely granular precipitate on the mitochondrial cristae and on the central vacuolar membrane, and, if present, on the vacuolar contents. Fixation should be kept to a minimum and prolonged incubation times up to 2 hr are necessary to show these reactive sites. The reaction appears to be strongly substrate-dependent and not affected by cyanide. Exposure of C. albicans cells to the antimycotic miconazole resulted in a strong increase in reduced nicotinamide, adenine dinucleotide and oxidase activity. The hypothesis is put forward that this enzyme, together with peroxidative and catalatic enzymes, may be implicated in the mechanism by which miconazole exerts its lethal effect on C. albicans.

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Reconstitution of Reduced Nicotinamide Adenine Dinucleotide Oxidase Activity with Menadione in Membrane Vesicles from the Menaquinone-Deficient Bacillus subtilis AroD. Relation between Electron Transfer and Active Transport

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1976.tb10699.x ◽

1976 ◽

Vol 67 (2) ◽

pp. 357-365 ◽

Cited By ~ 24

Author(s):

Arnold BISSCHOP ◽

Wil N. KONINGS

Keyword(s):

Electron Transfer ◽

Bacillus Subtilis ◽

Active Transport ◽

Nicotinamide Adenine Dinucleotide ◽

Oxidase Activity ◽

Membrane Vesicles ◽

Nicotinamide Adenine ◽

Reduced Nicotinamide Adenine Dinucleotide

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Soluble reduced nicotinamide adenine dinucleotide oxidase from Bacillus cereus T spores and vegetative cells. I. Purification

Canadian Journal of Microbiology ◽

10.1139/m69-237 ◽

1969 ◽

Vol 15 (11) ◽

pp. 1309-1312 ◽

Cited By ~ 5

Author(s):

D. H. Ashton ◽

L. C. Blankenship

Keyword(s):

Bacillus Cereus ◽

Nicotinamide Adenine Dinucleotide ◽

Gel Electrophoresis ◽

Oxidase Activity ◽

Vegetative Cell ◽

Nicotinamide Adenine ◽

Vegetative Cells ◽

Cell Extracts ◽

Cell Enzyme ◽

Reduced Nicotinamide Adenine Dinucleotide

Spores and vegetative cells of Bacillus cereus T were disrupted by two procedures and soluble extracts prepared from the ruptured cells. Reduced nicotinamide adenine dinucleotide (NADH2) oxidases were purified from the extracts by ammonium sulfate fractionation, ion exchange on hydroxylapatite, and preparative acrylamide gel electrophoresis. The electrophoresis step revealed the presence of two distinct components with NADH2 oxidase activity in soluble extracts of spores while vegetative cell extracts contained only one. The faster moving component in spore extracts constituted about 30% of the NADH2 oxidase activity recovered and was identical with the vegetative cell enzyme in electrophoretic mobility on acrylamide gel. The slower moving spore component accounted for 70% of recovered activity and was found in soluble extracts regardless of the procedure used to rupture spores.

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