Transient potentiometry based d-serine sensor using engineered d-amino acid oxidase showing quasi-direct electron transfer property

2021 ◽  
pp. 113927
Author(s):  
Shouhei Takamatsu ◽  
Inyoung Lee ◽  
Jinhee Lee ◽  
Ryutaro Asano ◽  
Wakako Tsugawa ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Amino Acid ◽  
Direct Electron Transfer ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Transfer Property

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 The carbanion of nitroethane is an inhibitor of, and not a substrate for, flavocytochrome b2 [l-(+)-lactate dehydrogenase]

1990 ◽  
Vol 266 (1) ◽  
pp. 301-304 ◽  
Author(s):  
R Genet ◽  
F Lederer
Keyword(s):  
Electron Transfer ◽  
Amino Acid ◽  
Lactate Dehydrogenase ◽  
Active Site ◽  
Competitive Inhibitor ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Flavocytochrome B2 ◽  
Enzyme Substrate

Although nitroethane does not bind to the active site of flavocytochrome b2, its anion, ethane nitronate, behaves as a competitive inhibitor, with a Ki of 2.2 mM. No electron transfer can be detected between the nitronate and the enzyme, in contrast with the observations of other workers on D-amino acid oxidase. Propionate is a competitive inhibitor, with a Ki of 28 mM. The significance of these results with respect to the proposed carbanion mechanism and the putative existence of a covalent enzyme-substrate intermediate is discussed.

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