Kinetics of enzymic oxidation of indoleacetic acid (IAA) are interpreted as indicating that the reaction has an autocatalytic, cyclical mechanism involving unstable intermediates whose formation and disappearance are important in determining the over-all reaction rate. The kinetics do not support the idea that IAA oxidation occurs mainly by reaction with Mn+3, nor that the reaction is an electron transfer from IAA to O2 catalyzed by a pcroxidase-H2O2-Mn+2 complex, nor that Mn is essential to the reaction. H2O2 is probably not a major reaction intermediate. One-electron oxidation of IAA by peroxidase giving a free radical, followed by spontaneous reaction of the radical with oxygen to give a peroxy oxidant which can reoxidize the peroxidase ...
The reactions of permanganate ion with seven -amino acids in aqueous KH2PO4-K2HPO4 buffers have been...
The inactivation of peroxidases by its oxidant substrate H2O2 limits the usefulness of these versati...
The inactivation of peroxidases by its oxidant substrate H2O2 limits the usefulness of these versati...
The indoleacetic acid (IAA)-oxidizing enzyme preparation from Omphalia flavida exhibits peroxidase a...
NOTE: Text or symbols not renderable in plain ASCII are indicated by [...]. Abstract is included in ...
A mechanistic model of peroxidase-catalyzed oxidation of indole-3-acetic acid (IAA) at neutral pH ha...
The heme enzyme indoleamine 2,3-dioxygenase (IDO1) catalyzes L-Trp oxidation in non-hepatic mammalia...
A study has been made of the reaction mechanism of a model system for enzymatic hydroxylation. The ...
The kynurenine pathway is the major route of l-tryptophan (l-Trp) catabolism in biology, leading ult...
Steady-state kinetic data for monoamine oxidase A in crude extracts suggest an exclusively ping-pong...
The kinetics of the glucose oxidase-catalyzed reaction of glucose with O2, which produces gluconic a...
ABSTRACT. Kinetics of oxidation of indole by peroxomonosulphate (PMS) in aqueous acetonitrile medium...
Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes t...
To understand the mechanism of a biological oxidation in which oxygen is incorporated into a substra...
Indoleamine 2, 3-dioxygenase (IDO) is a type-b heme enzyme responsible for catalyzing the reaction o...
The reactions of permanganate ion with seven -amino acids in aqueous KH2PO4-K2HPO4 buffers have been...
The inactivation of peroxidases by its oxidant substrate H2O2 limits the usefulness of these versati...
The inactivation of peroxidases by its oxidant substrate H2O2 limits the usefulness of these versati...
The indoleacetic acid (IAA)-oxidizing enzyme preparation from Omphalia flavida exhibits peroxidase a...
NOTE: Text or symbols not renderable in plain ASCII are indicated by [...]. Abstract is included in ...
A mechanistic model of peroxidase-catalyzed oxidation of indole-3-acetic acid (IAA) at neutral pH ha...
The heme enzyme indoleamine 2,3-dioxygenase (IDO1) catalyzes L-Trp oxidation in non-hepatic mammalia...
A study has been made of the reaction mechanism of a model system for enzymatic hydroxylation. The ...
The kynurenine pathway is the major route of l-tryptophan (l-Trp) catabolism in biology, leading ult...
Steady-state kinetic data for monoamine oxidase A in crude extracts suggest an exclusively ping-pong...
The kinetics of the glucose oxidase-catalyzed reaction of glucose with O2, which produces gluconic a...
ABSTRACT. Kinetics of oxidation of indole by peroxomonosulphate (PMS) in aqueous acetonitrile medium...
Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes t...
To understand the mechanism of a biological oxidation in which oxygen is incorporated into a substra...
Indoleamine 2, 3-dioxygenase (IDO) is a type-b heme enzyme responsible for catalyzing the reaction o...
The reactions of permanganate ion with seven -amino acids in aqueous KH2PO4-K2HPO4 buffers have been...
The inactivation of peroxidases by its oxidant substrate H2O2 limits the usefulness of these versati...
The inactivation of peroxidases by its oxidant substrate H2O2 limits the usefulness of these versati...