Hydrazone formation of 2,4‐dinitrophenylhydrazine with pyrroloquinoline quinone in porcine kidney diamine oxidase

Meer, Robert A. van der; Jongejan, Jaap A.; Frank, Johannes; Duine, J. A.; Duine, J.A.

doi:10.1016/0014-5793(86)81350-3

Cited by 76 publications

(21 citation statements)

References 8 publications

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“…Recent work has established that PQQ, or a closely similar derivative, is the bound organic cofactor in mammalian copper-containing amine oxidases [3][4][5][6][7][8][9]. The optical absorption spectrum of the free PQQ semiquinone has been measured in solution [19]; intense bands occur at 460 and 360 rim.…”

Section: Discussionmentioning

confidence: 99%

“…Even though each of these enzymes exhibits preferential activity for different substrates, they all nevertheless contain divalent copper and a covalently bound organic co factor, pyrroloquinolinequinone (PQQ) [3][4][5][6][7][8][9]. When amine substrates are added under anaerobic or lowtemperature conditions to plant diamine oxidases, a spectral intermediate with characteristic electronic absorption bands at 465,430 and 360 nm is observed [10][11][12].…”

Section: Introductionmentioning

confidence: 99%

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The generation of an organic free radical in substrate‐reduced pig kidney diamine oxidase‐cyanide

et al. 1987

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When the cyanide complex of the copper protein, pig kidney diamine oxidase, is reduced anaerobically by cadaverine (1,5-diaminopentane), the broad, 480 nm absorption band characteristic of the resting enzyme is bleached and a new absorption spectrum with features at 457, 429, 403 (shoulder), 360 (shoulder) and 332 nm appears. Concomitantly, the EPR spectrum of the enzyme Cu(II)-CN complex decreases in intensity and a new signal is observed that is attributable to an organic free radical. The g values and hyperfine splittings are similar to those previously assigned to a free radical observed when the cyanide complex of lentil seedling diamine oxidase is reacted with the substrate p-dimethylaminomethylbenzylamine [(1984) FEBS Lett. 176, 378 380]. The optical absorption and EPR spectra of the organic radical observed in both proteins are consistent with the same semiquinone-type structure, as expected if pyrroloquinolinequinone (PQQ) is the bound cofactor found in both enzymes.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The generation of an organic free radical in substrate‐reduced pig kidney diamine oxidase‐cyanide

et al. 1987

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“…[25] and references therein). Application of the hydrazine method, revealed indeed only 1 covalently bound PQQ per enzyme molecule [16,19]. However, from titration experiments with substrate for bovine plasma amine oxidase purified by a novel method [26], it has been claimed that 2 PQQ's are present [26].…”

Section: Discussionmentioning

confidence: 99%

“…The acetone adduct of PQQ [ 141, PQQHz [ 151, PQQ-oxazole from glycine [9], the hydrazone of PQQ and 2,4_dinitrophenylhydrazine [16], and a PQQ-tryptophan condensation product [17] were prepared as described. Bovine serum albumin was from Sigma (crystallized and lyophilized, product no.…”

Section: Chemicalsmentioning

confidence: 99%

Determination of PQQ in quinoproteins with covalently bound cofactor and in PQQ‐derivatives

et al. 1989

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Application of the so-called hexanol extraction procedure for PQQ determination, originally based on detachment of the cofactor from quinoproteins and conversion into PQQ-S,S-dihexyl ketal, leads in several cases to a number of products due to uncontrollable esterification. The present modified procedure, detaching the covalently bound cofactor and converting it into 4-hydroxy-5-hexoxy-pyrroloquinoline, was tested on a number of proteins. Only the expected product was obtained for the known quinoproteins, in a quantitative yield, as revealed by comparison with the values determined with the hydrazine method. Thus this independent method confirmed that bovine serum amine oxidase, porcine kidney diamine oxidase, dopamine /I-hydroxylase from bovine adrenal medulla, methylamine dehydrogenase from Thiobncillus versutus, glutamate decarboxylase from Escherichiu coli, and 3,4dihydroxyphenylalanine decarboxylase from pig kidney are really quinoproteins. Quantitative conversion was also achieved for condensation and addition products of PQQ (PQQ-acetone, PQQH,, PQQ-oxaxole, PQQ-dinitrophenylhydraxone, and PQQ-tryptophan). In view of this conversion and the fact that catalytic activity of PQQ is not required, the method seems suited to investigate the distribution of the cofactor in eukaryotes, especially in mammals where it is almost certain that PQQ occurs only in derivatized form. Finally, just like the hydrazine method, the hexanol extraction procedure seems unable to keep the structure of the cofactor as it exists in the active site, intact, as demonstrated for the pro-PQQ cofactor of methylamine dehydrogenase.

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“…Extraction of the pronase digest on an ODS cartridge was performed according to Van der Meer et al [18]. As the hydrazine adducts of PQQ appeared to elute from the ODS column in the 10% methanol washing step, this step was omitted.…”

Section: Methodsmentioning

confidence: 99%

Soybean lipoxygenase‐1 is not a quinoprotein

et al. 1990

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Soybean lipoxygenase-1 was reinvestigated with respect to its quinoprotein nature. It has been reported previously that soybean lipoxygenase-1 contains pyrroloquinoline quinone as the organic cofactor [I]. Because spectroscopic data were found to be inconsistent [2] with the evidence presented in [l], we sought to reproduce the published data by carefully following the procedures described in [l] and supplementing them with new analytical results. The combined data lead us to conclude that soybean lipoxygenase-I is not a quinoprotein.

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Hydrazone formation of 2,4‐dinitrophenylhydrazine with pyrroloquinoline quinone in porcine kidney diamine oxidase

Cited by 76 publications

References 8 publications

The generation of an organic free radical in substrate‐reduced pig kidney diamine oxidase‐cyanide

The generation of an organic free radical in substrate‐reduced pig kidney diamine oxidase‐cyanide

Determination of PQQ in quinoproteins with covalently bound cofactor and in PQQ‐derivatives

Soybean lipoxygenase‐1 is not a quinoprotein

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