Direct electrical communication between chemically modified enzymes and metal electrodes. 2. Methods for bonding electron-transfer relays to glucose oxidase and D-amino-acid oxidase

1988 ◽  
Vol 110 (8) ◽  
pp. 2615-2620 ◽  
Author(s):  
Yinon. Degani ◽  
Adam. Heller
Keyword(s):  
Electron Transfer ◽  
Amino Acid ◽  
Glucose Oxidase ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Metal Electrodes ◽  
Chemically Modified ◽  
Bonding Electron

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.

Ultrafast photoinduced electron transfer in o-aminobenzoate – D-amino acid oxidase complex

2021 ◽  
pp. 113448
Author(s):  
Seiji Taniguchi ◽  
Haik Chosrowjan ◽  
Haruhiko Tamaoki ◽  
Yasuzo Nishina ◽  
Arthit Nueangaudom ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Amino Acid ◽  
Photoinduced Electron Transfer ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

Theoretical analyses of the fluorescence lifetimes of the d-amino acid oxidase–benzoate complex dimer from porcine kidney: molecular dynamics simulation and photoinduced electron transfer

RSC Advances ◽  
2014 ◽  
Vol 4 (96) ◽  
pp. 54096-54108 ◽  
Author(s):  
Arthit Nueangaudom ◽  
Kiattisak Lugsanangarm ◽  
Somsak Pianwanit ◽  
Sirirat Kokpol ◽  
Nadtanet Nunthaboot ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Electron Transfer ◽  
Amino Acid ◽  
Molecular Dynamics Simulation ◽  
Photoinduced Electron Transfer ◽  
Aromatic Amino Acids ◽  
Dynamics Simulation ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Electron Transfer Theory

The mechanism of photoinduced electron transfer from benzoate and aromatic amino acids to the excited isoalloxazine in the d-amino acid oxidase–benzoate complex dimer was studied using molecular dynamics simulation and an electron transfer theory.

scholarly journals Mechanisms of Reaction of Some Flavoprotein Enzymes with Oxygen

1965 ◽  
Vol 49 (1) ◽  
pp. 201-211
Author(s):  
Quentin H. Gibson
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Glucose Oxidase ◽  
Intermediate Formation ◽  
Reduced Form ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Cytochrome C Reductase ◽  
Two Stages ◽  
Reduced Forms

Biochemical investigations of the properties of free flavins and of flavoproteins have shown that reduction usually occurs in two stages, with the intermediate formation of semiquinones in the case of free flavins. Flavoproteins often show spectroscopically similar intermediates, when partially reduced with substrate. These may, however, be enzyme-product complexes. Detailed investigation of individual flavoprotein enzymes has shown examples in which catalysis involves transition of the enzyme between oxidized and fully reduced forms (glucose oxidase), between oxidized and intermediate forms (D-amino acid oxidase), and intermediate and fully reduced forms (TPNH—cytochrome c reductase). Further, examples are known in which both intermediate and reduced forms react with oxygen, in which only one reacts, while in TPNH—cytochrome c reductase neither the intermediate nor the reduced form reacts with molecular oxygen. The physiological significance of these complex findings is uncertain, partly because it is not known whether purified flavoproteins occur in the same form in the tissues. It seems unlikely, however, that flavoproteins make a major contribution to the respiratory exchange of mammals.

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