Effect of metal substitution on the chromophore of bovine serum amine oxidase

Suzuki, Shinnichiro; Sakurai, Takeshi; Nakahara, Akitsugu; Manabe, Takashi; Okuyama, Tsuneo

doi:10.1021/bi00276a016

Cited by 78 publications

(86 citation statements)

References 26 publications

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“…Reconstitution of copper-depleted BSAO with Co(II) was found to restore some amine oxidase activity (57,65,66). Since the Co(II)-derivative cannot form a semiquinone radical intermediate, the finding that Co(II)-BSAO is catalytically competent suggests that the Cu(I)-semiquinone is not an obligatory intermediate of the catalytic pathway.…”

Section: Reactivity Of Tpq Models Toward Aminesmentioning

confidence: 99%

“…In enzymes, the bound copper has been proposed to play an essential role in the reoxidation of the substrate-reduced cofactor (57,58), and a similar function is, in principle, conceivable also for model systems. As already been noted, the presence of (bpy)Cu(II) has been reported to be an essential ingredient for the aerobic deamination of benzylamine by topa (28).…”

Section: Reactivity Of Tpq Models Toward Aminesmentioning

confidence: 99%

“…Since the Co(II)-derivative cannot form a semiquinone radical intermediate, the finding that Co(II)-BSAO is catalytically competent suggests that the Cu(I)-semiquinone is not an obligatory intermediate of the catalytic pathway. On the basis of these findings, the metal ion in BSAO was suggested to have a structural function, i.e., to maintain the active site in a proper conformation, rather than being directly involved in amine oxidation (57,65). More recently, Sue and Klinman conducted a very detailed study on the oxidative-half reaction of BSAO and proposed a passive role of copper in the reoxidation of reduced cofactor by molecular oxygen (67).…”

Section: Reactivity Of Tpq Models Toward Aminesmentioning

confidence: 99%

See 2 more Smart Citations

Modeling Novel Quinocofactors: An Overview

Rinaldi

Rescigno

Rinaldi

et al. 1999

Bioorganic Chemistry

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Section: Reactivity Of Tpq Models Toward Aminesmentioning

confidence: 99%

Section: Reactivity Of Tpq Models Toward Aminesmentioning

confidence: 99%

Section: Reactivity Of Tpq Models Toward Aminesmentioning

confidence: 99%

See 1 more Smart Citation

Modeling Novel Quinocofactors: An Overview

Rinaldi

Rescigno

Rinaldi

et al. 1999

Bioorganic Chemistry

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“…The maximum absorbance observed for BSAO is at 476 nm, whereas in lentil seedling enzyme the red band is shifted to 498 nm; this difference is probably due to specific interactions with amino acid residues in the active sites. The extinction coefficients were determined to be 476 = 3.8 mM -1 cm -1 and 278 = 261 mM -1 cm -1 for BSAO [12,13], while for LSAO the corresponding values were 498 = 4.1 mM -1 cm -1 and 278 = 245 mM -1 cm -1 [14]. visible absorption band depends on several electronic transitions.…”

Section: The Reaction Mechanism: the Reductive Half-reactionmentioning

confidence: 99%

Copper/topaquinone-containing amine oxidase from lentil seedlings and bovine plasma: Catalytic mechanism and energetic domains

Medda

Longu

Agostinelli

et al. 2004

JICS

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In this review the characteristics of the prosthetic group and the role of copper in amine oxidase purified from lentil seedlings are compared with the corresponding features of the amine oxidase isolated from bovine serum. Although both enzymes contain the same organic cofactor, the 6-hydroxydopa ( 2,4,5-trihydroxyphenethylamine) quinone, the catalytic cycle of lentil seedling amine oxidase operates through a Cu(I)-free-radical intermediate of the cofactor, whereas in bovine serum enzyme the radical form was not observed. The role of the metal in the catalytic mechanism of the two enzymes is also discussed. Moreover, the energetic domains and the effect of the temperature on activity, for both enzymes, are examined using differential scanning calorimetry

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“…Methoxatin contains electrophilic carbonyl groups and displays one-and two-electron redox chemistry (31). In this context it should be noted that free radicals have been detected in some amine oxidase reactions (32) and that sequential one-electron steps may be involved in the reoxidation of substrate-reduced amine oxidases by°2 (33)(34)(35)(36)(37). Several properties of methoxatin that are relevant to its potential functions in amine metabolism have already been 1 delineated.…”

mentioning

confidence: 99%

Evidence for methoxatin (pyrroloquinolinequinone) as the cofactor in bovine plasma amine oxidase from resonance Raman spectroscopy.

Moog¹,

McGuirl²,

Coté³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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Resonance Raman spectra of the 2,4-dinitrophenylhydrazine derivatives of bovine plasma amine oxidase [amine:oxygen oxidoreductase (deaminating) (copper-containing), EC 1.4.3.6] have been measured. Detailed comparisons to the spectra of the corresponding derivatives of methoxatin (pyrroloquinolinequinone), pyridoxal, and other aldehydes and diones provide further evidence that covalently bound methoxatin or a closely similar derivative is the organic cofactor in copper-containing amine oxidases. COOHCopper-containing amine oxidases [amine:oxygen oxidoreductase (deaminating) (copper-containing), EC 1.4.3.6] are a widespread and diverse class of enzymes. They can be isolated from microorganisms, plants, and mammals (1, 2). A variety of primary amines, including mono-, di-, and polyamines, can serve as substrates, depending on the enzyme source. In addition to copper, these amine oxidases also contain an organic cofactor that is tightly bound, probably covalently, to the enzyme; recent experiments have established a subunit:copper:cofactor stoichiometry of 2:2:1 for most amine oxidases (1-8). Extensive spectroscopic and ligand binding studies have defined the basic structure of the copper sites (1, 2, 9-15). The presence of an organic cofactor was first inferred from the sensitivity of amine oxidases to carbonyl reagents-e.g., phenylhydrazine, semicarbazide, and hydroxylamine (16). Despite considerable effort, the organic cofactor has not been conclusively identified. Many different techniques have been brought to bear on this problem, but the results have often been ambiguous or even conflicting. For many years the most likely candidate for the cofactor was pyridoxal or a closely related derivative (1, 2, 17-24), but strong evidence against pyridoxal had also been reported (1,2,6,(25)(26)(27)(28). Knowles and Yadav (2) have summarized concisely and analyzed the available data in a recent review. In 1984 two groups independently presented spectroscopic (absorbance and fluorescence) and chromatographic evidence that methoxatin (pyrroloquinolinequinone, PQQ), structure 1, was the organic factor in copper-containing amine oxidases (29,30). Previously methoxatin had been identified as a coenzyme only in prokaryotic organisms (31). Methoxatin contains electrophilic carbonyl groups and displays one-and two-electron redox chemistry (31). In this context it should be noted that free radicals have been detected in some amine oxidase reactions (32) and that sequential one-electron steps may be involved in the reoxidation of substrate-reduced amine oxidases by°2 (33-37). Several properties of methoxatin that are relevant to its potential functions in amine metabolism have already been 1 delineated. For example, data pertaining to redox potentials, carbonyl chemistry, mechanisms of reactions with amines, and metal ion complexation are available for methoxatin and various analogues (38-41).The identification of the organic cofactor as methoxatin is potentially very important to understanding the mechanisms and functions ...

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Effect of metal substitution on the chromophore of bovine serum amine oxidase

Cited by 78 publications

References 26 publications

Modeling Novel Quinocofactors: An Overview

Modeling Novel Quinocofactors: An Overview

Copper/topaquinone-containing amine oxidase from lentil seedlings and bovine plasma: Catalytic mechanism and energetic domains

Evidence for methoxatin (pyrroloquinolinequinone) as the cofactor in bovine plasma amine oxidase from resonance Raman spectroscopy.

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