Electrochemistry of xanthine oxidase and its interaction with nitric oxide.
With the help of nanocrystalline TiO2, the direct electrochemistry of xanthine oxidase (XOD) was achieved and two pairs of redox waves were observed. The interaction between XOD and nitric oxide (NO) was also investigated. The experimental results reveal that NO can be reduced at a XOD-nano TiO2 film modified electrode. When the NO concentration was low, the reduced product, HNO, would inactivate the protein. However, when the NO concentration was high, HNO would continue to react with NO to form N2O2- and N3O3-, which would not inhibit XOD, and thus the amount of active protein did not decrease any further.
Zhou
Hui
H
Department of Biochemistry and National Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, PR China.
Xu
Yi
Y
Chen
Ting
T
Suzuki
Iwao
I
Li
Genxi
G
D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry; D002623:Chemistry Techniques, Analytical / Q000379:methods; D003460:Crystallization; D004563:Electrochemistry / Q000379:methods*; D004566:Electrodes; D004583:Electrons; D006418:Heme / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008892:Milk / Q000378:metabolism; D008956:Models, Chemical; D053758:Nanoparticles; D009569:Nitric Oxide / Q000737:chemistry*; D014025:Titanium / Q000737:chemistry; D014969:Xanthine Oxidase / Q000737:chemistry*
D001672:Biocompatible Materials; C009495:titanium dioxide; D009569:Nitric Oxide; D006418:Heme; D014025:Titanium; D014969:Xanthine Oxidase