The nature of the 4a-hydroperoxyflavin in the mammalian flavin-containing monooxygenase

Jones, Kenneth C.; Ballou, David P.

doi:10.1515/9783111521350-111

Cited by 5 publications

(1 citation statement)

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“…The reaction of flavin-4a-hydroperoxide with thioxane is 10 5 faster than that of t-butyl hydroperoxide [30]. Enzyme bound flavin-4a-hydroperoxides exhibit typical reactivities like the oxygenation of sulfur-containing substrate analogs by the aromatic hydroxylases [36], by N,S-monooxygenase [37], and by cyclohexanone monooxygenase [38]. The latter performs catalysis by a Baeyer-Villiger mechanism including the monoxygenation of boronic acids to the corresponding alcohols.…”

Section: The Chemical Reactivity Of Luciferase Bound Flavin-4a-hydropmentioning

confidence: 99%

On the chemical mechanisms of bacterial luciferase, an updating

Ghisla¹,

Eckstein²,

Macheroux³

1987

Flavins and Flavoproteins 1987

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Section: The Chemical Reactivity Of Luciferase Bound Flavin-4a-hydropmentioning

confidence: 99%

On the chemical mechanisms of bacterial luciferase, an updating

Ghisla¹,

Eckstein²,

Macheroux³

1987

Flavins and Flavoproteins 1987

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Oxygen Activation by Flavins and Pterins

Palfey¹,

Ballou²,

Massey³

1995

Active Oxygen in Biochemistry

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Mechanisms of flavoprotein-catalyzed reactions

Ghisla¹,

Massey²

1989

EJB Reviews 1989

100

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Flavoproteins are a class of enzymes catalyzing a very broad spectrum of redox processes by different chemical mechanisms. This review describes the best studied of these mechanisms and discusses factors possibly governing reactivity and specificity.A large number of flavin-containing enzymes, several hundreds, has been uncovered to date. An unusual feature of flavoproteins is the variety of the catalytic reactions performed, which range from typical redox catalysis such as the dehydrogenation of an amino acid, or the activation of dioxygen, to photochemistry; from 'DNA damage repair' to light emission. These few examples illustrate the fact that the same coenzyme is able to catalyze, or take part in catalytic events which must vary widely from a mechanistic point of view. The chemistry underlying the conversion itself will be quite different from case to case. This versatility sets flavoproteins apart from most other cofactor-dependent enzymes, which, in general, each catalyze a single type of chemical reaction. The activation or 'steering' of a particular activity of the flavin results from the interaction with the protein at the active center. On the other hand, for the vast majority of these enzymes a common feature exists, that at some stage during the catalytic event a transfer of electrons takes place between the substrate and the flavin itself.The purpose of the present review is not to enumerate the different functions of flavoproteins, this having been done elsewhere [l -41, but to focus on the mechanisms of catalysis, and on the possible ways of interaction of the flavin nucleus with the protein, i.e. on how this brings about chemistry appropriate to the particular enzyme reaction. In order toCorrespondence to S. Ghisla,

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The nature of the 4a-hydroperoxyflavin in the mammalian flavin-containing monooxygenase

Cited by 5 publications

References 0 publications

On the chemical mechanisms of bacterial luciferase, an updating

On the chemical mechanisms of bacterial luciferase, an updating

Oxygen Activation by Flavins and Pterins

Mechanisms of flavoprotein-catalyzed reactions

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