A theoretical study of the dioxygen activation by glucose oxidase and copper amine oxidase.
Glucose oxidase (GO) and copper amine oxidase (CAO) catalyze the reduction of molecular oxygen to hydrogen peroxide. If a closed-shell cofactor (like FADH(2) in GO and topaquinone (TPQ) in CAO) is electron donor in dioxygen reduction, the formation of a closed-shell species (H(2)O(2)) is a spin forbidden process. Both in GO and CAO, formation of a superoxide ion that leads to the creation of a radical pair is experimentally suggested to be the rate-limiting step in the dioxygen reduction process. The present density functional theory (DFT) studies suggest that in GO, the creation of the radical pair induces a spin transition by spin orbit coupling (SOC) in O(2)(-)(rad), whereas in CAO, it is induced by exchange interaction with the paramagnetic metal ion (Cu(II)). In the rate-limiting step, this spin-transition is suggested to transform the O(2)(-)(rad)-FADH(2)(+)(rad) radical pair in GO and the Cu(II)-TPQ (triplet) species in CAO, from a triplet (T) to a singlet (S) state. For CAO, a mechanism for the O[bond]O cleavage step in the biogenesis of TPQ is also suggested.
Prabhakar
Rajeev
R
Department of Physics, Stockholm Centre for Physics, Astronomy and Biotechnology (SCFAB), Stockholm University, S-106 91 Stockholm, Sweden.
Siegbahn
Per E M
PE
Minaev
Boris F
BF
D006631:Amine Oxidase (Copper-Containing) / Q000378:metabolism*; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives* / Q000378:metabolism; D005949:Glucose Oxidase / Q000378:metabolism*; D013481:Superoxides / Q000378:metabolism*
C086758:2,4,5-trihydroxyphenylalanine quinone; D013481:Superoxides; D004295:Dihydroxyphenylalanine; D005949:Glucose Oxidase; D006631:Amine Oxidase (Copper-Containing)