Title : Superoxide production by dinitrophenyl-derivatized thioredoxin reductase--a model for the mechanism and correlation to immunostimulation by dinitrohalobenzenes.

Pub. Date : 1999

PMID : 10609886






2 Functional Relationships(s)
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1 A model explaining the reactivity of dinitrohalobenzenes with thioredoxin reductase is presented, involving dinitrophenyl-derivatization of both the selenocysteine residue and its neighboring cysteine residue, reduction by NADPH of the enzyme-bound flavin in dinitrophenyl-alkylated enzyme (dnp-TrxR), followed by two consecutive one-electron transfers from the flavin to nitro groups of the dnp-moieties in dnp-TrxR, forming nitro anion radicals. 4,6-dinitro-o-cresol thioredoxin Homo sapiens
2 A model explaining the reactivity of dinitrohalobenzenes with thioredoxin reductase is presented, involving dinitrophenyl-derivatization of both the selenocysteine residue and its neighboring cysteine residue, reduction by NADPH of the enzyme-bound flavin in dinitrophenyl-alkylated enzyme (dnp-TrxR), followed by two consecutive one-electron transfers from the flavin to nitro groups of the dnp-moieties in dnp-TrxR, forming nitro anion radicals. 4,6-dinitro-o-cresol thioredoxin Homo sapiens