AbstractAscorbate-dependent detoxification of hydrogen peroxide by guaiacol-type peroxidases is increased considerably in the presence of 3,4-dihydroxyphenolic compounds, suggesting that ascorbate is the natural substrate for many types of peroxidase in situ and not just the ascorbate-specific peroxidases. The ascorbate-dependent destruction of hydrogen peroxide in the more acidic cellular compartments such as the vacuole may be an important function of such non-specific peroxidases. The stress-induced production of phenolic compounds would render the guaiacol peroxidases in other less acidic-cellular sites effective as ascorbate-dependent H2O2-detoxifying enzymes
Plant peroxidases (class III peroxidases) are present in all land plants. They are members of a larg...
Peroxidases catalyze many reactions, the most common being the utilization of H2O2 to oxidize numero...
It was shown that basipetal retardation of cell elongation in the growth zone of etiolated maize me...
Plants have to counteract unavoidable stress-caused anomalies such as oxidative stress to sustain th...
Hydrogen peroxide (H2O2), an important relatively stable non-radical reactive oxygen species (ROS) i...
Switchgrass (Panicum virgatum L.) is being developed as a bioenergy species. Recently an early versi...
When plants are exposed to stressful environmental conditions, the production of Reactive Oxygen Spe...
A proportion of the plant's L-ascorbate (vitamin C) occurs in the apoplast, where it and its metabol...
The aqueous phase of the cell walls inside leaves (apoplast) of spinach contained ascorbate (AA) and...
Regular exploitation of rubber trees by tapping, a wounding process, leads to an increase in the pro...
AbstractMethylviologen (MV) induces oxidative damages in leaves. In order to understand its mechanis...
AbstractTo analyze the potential of the active oxygen-scavenging system of chloroplasts, we introduc...
Hydrogen peroxide (H2O2), an important relatively stable non-radical reactive oxygen species (ROS) i...
Abstract: Hydrogen peroxide (H2O2), an important relatively stable non-radical reactive oxygen speci...
Ascorbic acid oxidase (AAO) has been fully characterized at molecular level, yet its functional role...
Plant peroxidases (class III peroxidases) are present in all land plants. They are members of a larg...
Peroxidases catalyze many reactions, the most common being the utilization of H2O2 to oxidize numero...
It was shown that basipetal retardation of cell elongation in the growth zone of etiolated maize me...
Plants have to counteract unavoidable stress-caused anomalies such as oxidative stress to sustain th...
Hydrogen peroxide (H2O2), an important relatively stable non-radical reactive oxygen species (ROS) i...
Switchgrass (Panicum virgatum L.) is being developed as a bioenergy species. Recently an early versi...
When plants are exposed to stressful environmental conditions, the production of Reactive Oxygen Spe...
A proportion of the plant's L-ascorbate (vitamin C) occurs in the apoplast, where it and its metabol...
The aqueous phase of the cell walls inside leaves (apoplast) of spinach contained ascorbate (AA) and...
Regular exploitation of rubber trees by tapping, a wounding process, leads to an increase in the pro...
AbstractMethylviologen (MV) induces oxidative damages in leaves. In order to understand its mechanis...
AbstractTo analyze the potential of the active oxygen-scavenging system of chloroplasts, we introduc...
Hydrogen peroxide (H2O2), an important relatively stable non-radical reactive oxygen species (ROS) i...
Abstract: Hydrogen peroxide (H2O2), an important relatively stable non-radical reactive oxygen speci...
Ascorbic acid oxidase (AAO) has been fully characterized at molecular level, yet its functional role...
Plant peroxidases (class III peroxidases) are present in all land plants. They are members of a larg...
Peroxidases catalyze many reactions, the most common being the utilization of H2O2 to oxidize numero...
It was shown that basipetal retardation of cell elongation in the growth zone of etiolated maize me...