Mitochondrial Monoamine Oxidase

Patek, David R.; Hellerman, Leslie

doi:10.1016/s0021-9258(19)42740-3

Cited by 73 publications

(8 citation statements)

References 33 publications

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“…The oxidation of the reduced flavin (FlEtH) with molecular oxygen occurs readily to give hydroperoxyflavins; 15 therefore, the crucial step of the catalytic cycle of Scheme 1 is the transformation of FlEt + to FlEtH with an appropriate reductant which may correspond to NADPH. We turned our attention on the fact that hydrazine derivatives are suicide inhibitors for flavoenzymes such as mammalian monoamine oxidase 16 and found that hydrazine monohydrate serves as an excellent reductant. Oxidation of methyl p-tolyl sulfide (5) with molecular oxygen (1 atm, balloon) in the presence of 1 mol % 3 and hydrazine monohydrate in TFE at room temperature gave the corresponding sulfoxide in >99% yield along with the generation of water and molecular nitrogen.…”

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confidence: 99%

“…Thus, hydrazine would attack at the 4a(C) position of the isoalloxazine ring of FlEt + to form the 4aadduct (FlEtNHNH 2 ), which undergoes β-elimination of diazene (NHdNH) to afford FlEtH. 16 Diazene thus formed again reacts with FlEt + similarly to give FlEtNdNH, which undergoes β-elimination to afford FlEtH and molecular nitrogen. The FlEtH thus formed would undergo reaction with molecular oxygen to form FlEtOOH to complete the catalytic cycle.…”

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Flavin Catalyzed Oxidations of Sulfides and Amines with Molecular Oxygen

et al. 2003

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Novel biomimetic, aerobic oxidation with an organocatalyst was performed. The oxidations of organic substrates such as sulfides, secondary amines, N-hydroxylamines, and tertiary amines with molecular oxygen (1 atm) or even in air in the presence of 5-ethyl-3-methyllumiflavinium perchlorate catalyst and hydrazine monohydrate in 2,2,2-trifluoroethanol occur highly efficiently to give the corresponding oxidized compounds in excellent yields along with water and molecular nitrogen, which are environmentally benign. The TON of the oxidation of sulfides amounts to 19 000.

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Flavin Catalyzed Oxidations of Sulfides and Amines with Molecular Oxygen

et al. 2003

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“…The reactive diimide would then become covalently attached to the enzyme (thus, hydrazines would qualify as "suicide" inactivators) (Abeles & Maycock, 1976). It has been shown that phenylhydrazine inactivates mitochondrial monoamine oxidase via the intermediate formation of phenyldiimide (Patek & Hellerman, 1974).…”

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Studies on the mechanism of action of plasma amine oxidase

Suva¹,

Abeles²

1978

Biochemistry

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“…Several of the effects of phenylhydrazine are oxygen-dependent. These include its inactivation of papain , amine oxidase (Patek and Hellerman, 1974), lactoperoxidase and triosephosphate dehydrogenase , horse radish peroxidase and thyroid peroxidase (Hidaka and , its inhibition of the respiration of mitochondria and of submitochondrial particles (Asami, 1968), and its desensitization of grasshopper muscle (McDonald, 1972). Aside from the involvement of phenyldiazene as an intermediate (Cauquis and Genies, 1968; Itano, 1970), the catalytic effect of Cu2+ (Eberson and Persson, 1962;Audrieth and Ogg, 1951) and the formation of H2O2 (Cohen and Hochstein, 1964; Audrieth and Ogg, 1951), very little is known about the air oxidation of phenylhydrazine in buffered aqueous solutions.…”

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The oxidation of phenylhydrazine: superoxide and mechanism

Misra¹,

Fridovich²

1976

Biochemistry

216

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The oxidation of phenylhydrazine in buffered aqueous solutions is a complex process involving several intermediates. It can be initiated by metal cations, such as Cu2+; in which case EDTA acts as an inhibitor. It can also be intiated by oxyhemoglobin; in which case chelating agents do not interfere. Superoxide radical is both a product of this reaction and a chain propagator. The formation of O2- could be demonstrated in terms of a reduction of nitroblue tetrazolium, which was prevented by superoxide dismutase. The importance of O2- in carrying the reaction chains was shown by the inhibition of phenylhydrazine oxidation by superoxide dismutase. Hydrogen peroxide accumulated during the reaction and could be detected with catalase. The progress of this oxidation could be monitored in terms of oxygen consumption and by following increases in absorbance at 280 or 320 nm. The oxidation was markedly autocatalytic and superoxide dismutase had the effect of extending the lag period. The absorbance at 280 nm was due to an intermediate which first accumulated and was then consumed. This intermediate appears to be benzendiazonium ion. The absorbance at 320 nm was due to a stable product, which was not identified. The time course of oxygen consumption paralleled the increase in absorbance at 320 nm and lagged behind the changes at 280 nm. Exogenous benzenediazonium ion accelerated the oxidation of phenylhydrazine and eliminated the lag phase. Benzenediazonium ion must therefore react with phenylhydrazine to produce a very reactive intermediate, possibly phenyldiazene. A mechanism was proposed which is consistent with the data. The intermediates and products of the oxidation of phenylhydrazine include superoxide radical, hydrogen peroxide, phenylhydrazyl radical, phenyldiazene, and benzenediazonium ion. This is a minimal list: others remain to be detected and identified. It appears likely that the diverse biological effects of phenylhydrazine are largely due to the reactivities of these intermediates and products.

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Mitochondrial Monoamine Oxidase

Cited by 73 publications

References 33 publications

Flavin Catalyzed Oxidations of Sulfides and Amines with Molecular Oxygen

Flavin Catalyzed Oxidations of Sulfides and Amines with Molecular Oxygen

Studies on the mechanism of action of plasma amine oxidase

The oxidation of phenylhydrazine: superoxide and mechanism

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