On the Mechanism of the Ascorbic Acid—Ascorbic Acid Oxidase Reaction. The Hydrogen Peroxide Question

1942 ◽  
Vol 64 (5) ◽  
pp. 1212-1219 ◽  
Author(s):  
Harry G. Steinman ◽  
Charles R. Dawson
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Acid Oxidase ◽  
Ascorbic Acid Oxidase ◽  
Oxidase Reaction

scholarly journals Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase

1980 ◽  
Vol 186 (1) ◽  
pp. 377-380 ◽  
Author(s):  
S Shigeoka ◽  
Y Nakano ◽  
S Kitaoka
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Electron Donor ◽  
Euglena Gracilis ◽  
Oxidase Activity ◽  
Acid Oxidase ◽  
Ascorbic Acid Oxidase ◽  
Reduction System ◽  
Oxidation Reduction ◽  
Euglena Gracilis Z

Euglena gracilis was found to contain a peroxidase that specifically require L-ascorbic acid as the natural electron donor in the cytosol. The presence of an oxidation-reduction system metabolizing L-ascorbic acid was demonstrated in Euglena cells. Oxidation of L-ascorbic acid by the peroxidase, and the absence of ascorbic acid oxidase activity, suggests that the system functions to remove H2O2 in E. gracilis, which lacks catalase.

Notizen: Effect of Magnetic Field on Ascorbic Acid Oxidase Activity, I

1986 ◽  
Vol 41 (3) ◽  
pp. 355-358 ◽  
Author(s):  
V. S. Ghole ◽  
P. S. Damle ◽  
W. H.-P. Thiemann
Keyword(s):  
Magnetic Field ◽  
Ascorbic Acid ◽  
Homogeneous Magnetic Field ◽  
Acid Oxidase ◽  
High Substrate Concentration ◽  
Ascorbic Acid Oxidase ◽  
Rate Of Reaction ◽  
Substrate Concentrations ◽  
Burk Plot

A homogeneous magnetic field of 1.1 T strength exhibits a significant influence on the activity of the enzyme ascorbic acid oxidase in vitro. A Lineweaver-Burk plot of the reaction shows the typical pattern of a mixed-type inhibition, i.e. a larger rate of reaction at low substrate concentrations and a smaller rate of reaction at high substrate concentration than that of the control without magnetic field applied.

scholarly journals Is Ceruloplasmin an Ascorbic Acid Oxidase?

1962 ◽  
Vol 237 (11) ◽  
pp. 3455-3457
Author(s):  
Anatol G. Morell ◽  
Philip Aisen ◽  
I. Herbert Scheinberg
Keyword(s):  
Ascorbic Acid ◽  
Acid Oxidase ◽  
Ascorbic Acid Oxidase

The Chemical Nature of "Ascorbic Acid Oxidase"

Science ◽  
1937 ◽  
Vol 86 (2219) ◽  
pp. 35-35
Author(s):  
Elmer H. Stotz ◽  
Carter J. Harrer ◽  
C. G. King
Keyword(s):  
Ascorbic Acid ◽  
Chemical Nature ◽  
Acid Oxidase ◽  
Ascorbic Acid Oxidase

scholarly journals Ascorbic Acid Oxidase in Barley Roots

1955 ◽  
Vol 30 (2) ◽  
pp. 174-181 ◽  
Author(s):  
S. I. Honda
Keyword(s):  
Ascorbic Acid ◽  
Acid Oxidase ◽  
Ascorbic Acid Oxidase

Nitroalkanes as Reductive Substrates for Flavoprotein Oxidases

1972 ◽  
Vol 27 (9) ◽  
pp. 1052-1053 ◽  
Author(s):  
David J. T. Porter ◽  
Judith G. Voet ◽  
Harold J. Bright
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Glucose Oxidase ◽  
Ph Dependence ◽  
Kinetic Mechanism ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Kinetics Of ◽  
Oxidase Reaction ◽  
Detailed Kinetic Mechanism

Nitroalkanes have been found to be general reductive substrates for D-amino acid oxidase, glucose oxidase and L-amino acid oxidase. These enzymes show different specificities for the structure of the nitroalkane substrate.The stoichiometry of the D-amino acid oxidase reaction is straightforward, consisting of the production of one mole each of aldehyde, nitrite and hydrogen peroxide for each mole of nitroalkane and oxygen consumed. The stoichiometry of the glucose oxidase reaction is more complex in that less than one mole of hydrogen peroxide and nitrite is produced and nitrate and traces of 1-dinitroalkane are formed.The kinetics of nitroalkane oxidation show that the nitroalkane anion is much more reactive in reducing the flavin than is the neutral substrate. The pH dependence of flavin reduction strongly suggests that proton abstraction is a necessary event in catalysis. A detailed kinetic mechanism is presented for the oxidation of nitroethane by glucose.It has been possible to trap a form of modified flavin in the reaction of D-amino acid oxidase with nitromethane from which oxidized FAD can be regenerated in aqueous solution in the presence of oxygen.

Phytochrome-mediated induction of ascorbic acid oxidase in mustard seedlings

1969 ◽  
Vol 56 (8) ◽  
pp. 417-417 ◽  
Author(s):  
M. van Poucke ◽  
F. Barthe ◽  
H. Mohr
Keyword(s):  
Ascorbic Acid ◽  
Acid Oxidase ◽  
Ascorbic Acid Oxidase
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