Purification and Properties of Three Separate Menadione Reductases from Hog Liver

Koli, Andrew K.; Yearby, Calvin; Scott, Winifred; Donaldson, Kenneth

doi:10.1016/s0021-9258(18)94400-5

Cited by 28 publications

(9 citation statements)

References 12 publications

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“…It is not as sensitive to dicoumarol as DT diaphorase. Inhibition in cell-free extracts occurs in the range 10 Ϫ5 M (Koli et al 1969). This is the same concentration range that was shown to effectively inhibit the neuronal Type II response in tissue sections.…”

Section: Dicoumarol-sensitive Nadph-dependent Enzymesmentioning

confidence: 73%

“…In contrast, the NADPH diaphorase activities of Type II neurons and of the diffuse blue band had a strong preference for ␤-NADPH over ␣-NADPH and were greatly attenuated by dicoumarol (Table 1). Taken together, these results indicate that the bulk of the neuronal Type I response was most likely produced by NOS (Hope and Vincent 1989) but that the neuronal Type II response, the diffuse blue band, and much of the cortical meshwork of fibers were most likely produced by DT diaphorase and/or NADPH dehydrogenase (quinone), and/or by a novel but similar enzyme (Levine et al 1960;Ernster et al 1962;Koli et al 1969;Dixon 1979). The neuronal Type II and diffuse blue band responses were easier to see at pH 8.5, but this was probably because the background was pale (relative to pH 6.8 and 7.4) and not because the responses were more intense at pH 8.5.…”

Section: Effects Of Chelators (N ϭ 3 Animals)mentioning

confidence: 90%

“…1.6.99.2) (Ernster et al 1962), and NADPH dehydrogenase (quinone) (E.C. 1.6.99.6) (Koli et al 1969). The other inhibitors had no effect on any of the staining.…”

Section: Effects Of Chelators (N ϭ 3 Animals)mentioning

confidence: 99%

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NOS- and Non-NOS NADPH Diaphorases in the Insular Cortex of the Syrian Golden Hamster

Wehby

Frank

1999

J Histochem Cytochem.

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We had previously shown NADPH diaphorase activity in fixed tissue slices of the insular cortex of the Syrian golden hamster (Mesocricetus auratus). The objective of this work was to determine the chemical identity of agents responsible for the observed NADPH diaphorase activities. Three different enzymatic NADPH diaphorase activities were distinguished in the insular cortex. (a) The activity seen in endothelial cells was not characterized histochemically, but it co-localized with eNOS-like immunoreactivity. (b) The neuronal Type I activity showed little sensitivity to 10(-5) M dicoumarol, could use either alpha- or beta-NADPH with almost equal facility, and co-localized with nNOS-like immunoreactivity. This activity was primarily attributable to nNOS. (c) The neuronal Type II activity was greatly attenuated by 10(-5) M dicoumarol, had a strong preference for beta-NADPH (rather than alpha-NADPH), and did not co-localize with any NOS-like immunoreactivity. These characteristics also apply to the NADPH diaphorase activity observed in the diffuse blue band in Layers II and III of agranular and dysgranular insular cortex and in the meshwork of cortical fibers. This staining was due primarily to a dicoumarol-sensitive dehydrogenase(s), either an isozyme of DT diaphorase (EC 1.6.99.2), or NADPH dehydrogenase (quinone) (EC 1.6. 99.6), or to a novel dicoumarol-sensitive NADPH dehydrogenase.

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Section: Dicoumarol-sensitive Nadph-dependent Enzymesmentioning

confidence: 73%

Section: Effects Of Chelators (N ϭ 3 Animals)mentioning

confidence: 90%

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NOS- and Non-NOS NADPH Diaphorases in the Insular Cortex of the Syrian Golden Hamster

Wehby

Frank

1999

J Histochem Cytochem.

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“…However, addition of menadione to mitochondria results in oxidation of intramitochondrial pyridine nucleotides (see Figure 4b). Since dicoumarol, a potent tool in investigating quinone reductases (Ernster et al, 1962;Koli et al, 1969), uncouples mitochondria, the mitochondrial enzymes involved in menadioneinduced pyridine nucleotide oxidatjon were investigated with mitochondrial extracts obtained with Triton X-100 (Table I). Although NADH and NADPH are equally good substrates for D,T-diaphorase (Ernster et al, 1962), in mitochondrial extracts NADPH is oxidized much more rapidly than NADH.…”

Section: Resultsmentioning

confidence: 99%

“…Besides D,T-diaphorase and NADPH-cytochrome P-450 reductase, the isolated enzyme NADH dehydrogenase can catalyze reduction of menadione (Iyanagi & Yamazaki, 1970). In addition, two diaphorases using NADH and NADPH as electron donors have been identified in hog liver cytoplasm (Koli et al, 1969). Their activities were characterized by use of the inhibitors dicoumarol and 2,4-dinitrophenol and by their reactivity toward various quinoid substrates.…”

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confidence: 99%

Menadione-(2-methyl-1,4-naphthoquinone) dependent enzymic redox cycling and calcium release by mitochondria

Frei¹,

Winterhalter²,

Richter³

1986

Biochemistry

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The results presented in this paper reveal the existence of three distinct menadione (2-methyl-1,4-naphthoquinone) reductases in mitochondria: NAD(P)H:(quinone-acceptor) oxidoreductase (D,T-diaphorase), NADPH:(quinone-acceptor) oxidoreductase, and NADH:(quinone-acceptor) oxidoreductase. All three enzymes reduce menadione in a two-electron step directly to the hydroquinone form. NADH-ubiquinone oxidoreductase (NADH dehydrogenase) and NAD(P)H azoreductase do not participate significantly in menadione reduction. In mitochondrial extracts, the menadione-induced NAD(P)H oxidation occurs beyond stoichiometric reduction of the quinone and is accompanied by O2 consumption. Benzoquinone is reduced more rapidly than menadione but does not undergo redox cycling. In intact mitochondria, menadione triggers oxidation of intramitochondrial pyridine nucleotides, cyanide-insensitive O2 consumption, and a transient decrease of delta psi. In the presence of intramitochondrial Ca2+, the menadione-induced oxidation of pyridine nucleotides is accompanied by their hydrolysis, and Ca2+ is released from mitochondria. The menadione-induced Ca2+ release leaves mitochondria intact, provided excessive Ca2+ cycling is prevented. In both selenium-deficient and selenium-adequate mitochondria, menadione is equally effective in inducing oxidation of pyridine nucleotides and Ca2+ release. Thus, menadione-induced Ca2+ release is mediated predominantly by enzymatic two-electron reduction of menadione, and not by H2O2 generated by menadione-dependent redox cycling. Our findings argue against D,T-diaphorase being a control device that prevents quinone-dependent oxygen toxicity in mitochondria.

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NADH Dehydrogenase (quinone)

Springer Handbook of Enzymes

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Purification and Properties of Three Separate Menadione Reductases from Hog Liver

Cited by 28 publications

References 12 publications

NOS- and Non-NOS NADPH Diaphorases in the Insular Cortex of the Syrian Golden Hamster

NOS- and Non-NOS NADPH Diaphorases in the Insular Cortex of the Syrian Golden Hamster

Menadione-(2-methyl-1,4-naphthoquinone) dependent enzymic redox cycling and calcium release by mitochondria

NADH Dehydrogenase (quinone)

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