α-α′-Dipyridyl or
            <i>Ortho</i>
            -Phenanthroline Stimulation of the Soluble Reduced Nicotinamide Adenine Dinucleotide Oxidase from
            <i>Bacillus subtilis</i>
            Spores and Dipicolinic Acid Inhibition of the Stimulated Enzyme

Tochikubo, Kunio

doi:10.1128/jb.117.3.1017-1022.1974

Cited by 10 publications

(4 citation statements)

References 8 publications

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“…Atebrine ( 5 mM) inhibited soluble NADH oxidase consistent with this reaction being flavoprotein-linked. Somewhat surprisingly antimycin A and 2-heptyl-4-hydroxyquinoline N-oxide were inhibitory to the soluble NADH oxidase, although Tochikubo [28] found that antimycin A inhibited the soluble NADH oxidase of Bacillus subtilis. Dipicolinic acid inhibited the soluble NADH oxidase of vegetative cells and spores although the spore activity Eur.…”

Section: Nadh Oxidase Activity Of the Soluble Fractionmentioning

confidence: 99%

Morphogenesis of the Membrane‐Bound Electron‐Transport System in Sporulating Bacillus megaterium KM

Wilkinson

1975

European Journal of Biochemistry

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The properties of electron transport systems present in soluble and particulate fractions of spores of Bacillus megaterium KM have been compared with those of similar fractions prepared from exponential-phase vegetative cells of this organism. The timing and localization of modifications of the electron transport system occurring during sporulation have been investigated by using a system for separating forespores from mother cells at all stages during development [8].Spore membranes contained cytochromes a + a3, b and o at lower concentrations than in vegetative membranes, and in addition cytochrome c, which was not found in exponential-phase vegetative membranes. An NADH oxidase activity of similar specific activity was found in both spore and vegetative membranes but DL-glycerol 3-phosphate and L-malate oxidase activities were found only in vegetative membranes. A soluble NADH oxidase of low specific activity was found in spores and vegetative cells which probably involves a flavoprotein reaction with oxygen because the activity was stimulated by FAD or FMN and difference spectra of concentrated soluble fractions showed spectra typical of a flavoprotein. Particulate NADH oxidase was sensitive to all classical inhibitors of electron transport tested whereas soluble NADH oxidase was insensitive to many of these inhibitors. Cytochrome c was formed between stage I and I1 of sporulation and this coincided with a five-fold increase in NADH-cytochrome c reductase activity. Forespore membranes had lower contents of cytochromes than sporangial cell membranes but similar levels of NADH and L-malate oxidases ; DL-glycerol 3-phosphate oxidase activity could not be detected in either membranes by stage 111 of sporulation. This characterization of spore electron transport systems provides a basis for suggestions concerning initial metabolic events during spore germination and the effect of a number of germination inhibitors.When placed in situations of nutritional limitation several Bacillus species are able to differentiate through a series of morphological and biochemical changes to produce a dormant form of the organism known as a spore which is resistant to a variety of physical and chemical treatments. We are interested in various aspects of the modification of structural features of organisms during sporulation and decided to investigate morphogenesis of the electron transport system during differentiation.Whilst the electron transport systems of bacteria have been extensively studied, little attention has been paid to spore electron transport. The data of Doi and Halvorson [4] indicated that extracts of the spores of Bacillus cereus strain T contained no cytochromes Enzymes. Malate oxidase (EC 1.1.3.3); DL-glycerol3-phosphate oxidase (EC 1.6.99.5); NADH-cytochrome c reductase (EC 1.6.99.3); ATPase (EC 3.6.1.3). and that electron transport was mediated by a soluble NADH-flavoprotein oxidase in contrast to the typical particulate cytochrome containing electron transport system of the vegetative organism. This work im...

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Section: Nadh Oxidase Activity Of the Soluble Fractionmentioning

confidence: 99%

Morphogenesis of the Membrane‐Bound Electron‐Transport System in Sporulating Bacillus megaterium KM

Wilkinson

1975

European Journal of Biochemistry

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“…Dipicolinic acid (pyridine 2,6-dicarboxylic acid, DPA) is present in nature as an oxidative degradation product of vitamins, coenzymes, and alkaloids. DPA shows various biological functions including activation/inactivation of some metalloenzymes , and inhibition of electron transport systems and acts as a potent inhibitor of low density lipoprotein oxidation . DPA is a desirable metal ion ligand because of its low toxicity and amphophilic nature.…”

Section: Introductionmentioning

confidence: 99%

Palladium(II) Complexes Containing Dipicolinic Acid (DPA), Iminodiacetic Acid (IDA), and Various Biologically Important Ligands

2009

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Ternary 1:1:1 complexes of Pd(II) with dipicolinic acid (DPA) or iminodiacetic acid (IDA) as primary ligands and some selected mono-and dicarboxylic amino acids (glycine, R-alanine, leucine, valine, phenylalanine, tryptophan, methionine, histadiene aspartic acid, and glutamic acid), aromatic carboxylic acids (salicylic and phthalic), and aliphatic carboxylic acids (succinic, oxalic, malic, maleic, malonic, and tartaric) as secondary ligands have been investigated by using the potentiometric technique at T ) 30 °C and I ) 0.1 mol • dm -3 . The ternary complexes are formed in a stepwise mechanism. Confirmation of the ternary complexes in solution has been carried out using conductometric measurements.

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“…As all samples other than the one mentioned above showed almost a linear time course in increase in optical density at 340 nm after the reaction was started, the specific activity was expressed as the value for nanomoles of NAD or NADP reduced per minute per milligram of protein obtained from the initial velocity. Soluble NADH oxidase [EC 1.6.99.2] and particulate NADH oxidase were assayed at 37 C by measuring the decrease in optical density at 340 nm of NADH as described previously (17,18); 0.3 /lmol of flavine mononucleotide was added to the assay cuvette containing soluble NADH oxidase. Alanine dehydrogenase [EC 1.4.1.1] and glucose-6-phosphate dehydrogenase [EC 1.1.1.49] were assayed at 37 C by measuring NADH and NADPH formation in optical density at 340 nm, respectively, as described previously (10,16); with glucose-f-phosphate dehydrogenase 0.1 /lmol of MgCl 2 was added to the assay cuvette.…”

mentioning

confidence: 99%

Effect of Disruption by Sonication under Different Conditions on the Activity of Glucose Dehydrogenase from Resting Spores of Bacillus subtilis

Tochikubo

Yasuda

1983

Microbiology and Immunology

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The activity of glucose dehydrogenase present in resting spores of Bacillus subtilis varied strikingly with the conditions for disrupting the spores by sonic treatment, namely, the time and strength of sonication, and the type and pH of the solution used for suspending the spores. When the resting spores were sonicated for 30 min at a current of 1.45 A in 100 mM phosphate buffer in the range of pH 6.0 to 6.6 or in deionized water, the enzyme activity of the former suspension was approximately 10 times higher than that of the latter suspension. However, the enzyme activity of the latter was markedly stimulated in the presence of sodium chloride. The glucose dehydrogenase from resting spores disrupted in 100 mM phosphate buffer (pH 6.6) was a salt-independent, active enzyme with a molecular weight of about 120,000, whereas the enzyme from resting spores disrupted in deionized water was a salt-dependent, inactive one with a molecular weight of about 55,000. A high concentration of dipicolinic acid strongly inhibited activation by a salt of inactive glucose dehydrogenase from resting spores in deionized water, suggesting one of its several important roles in vivo.

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α-α′-Dipyridyl or Ortho -Phenanthroline Stimulation of the Soluble Reduced Nicotinamide Adenine Dinucleotide Oxidase from Bacillus subtilis Spores and Dipicolinic Acid Inhibition of the Stimulated Enzyme

Cited by 10 publications

References 8 publications

Morphogenesis of the Membrane‐Bound Electron‐Transport System in Sporulating Bacillus megaterium KM

Morphogenesis of the Membrane‐Bound Electron‐Transport System in Sporulating Bacillus megaterium KM

Palladium(II) Complexes Containing Dipicolinic Acid (DPA), Iminodiacetic Acid (IDA), and Various Biologically Important Ligands

Effect of Disruption by Sonication under Different Conditions on the Activity of Glucose Dehydrogenase from Resting Spores of Bacillus subtilis

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