‘Thermodynamic’ mechanism of catalysis by haloperoxidases

FEBS Letters

Sal'nikov, Yury I.²  Kuz'mina, Natal'ya L.²  Ryabov, Alexander D.¹  Shevelkova, Angelina N.¹ 

[1] Department of Chemistry, M. V. Lomonosov Moscow State University, 000958 Moscow, Russia;Department of Chemistry, Kazan State University, 420008 Kazan, Russia

关键词: Haloperoxidase;    Catalysis;    Mechanism;    ClP;    chloroperoxidase from Caldariomyces fumago;    MCD;    monochlorodimedon;   

DOI  :  10.1016/0014-5793(96)00209-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel ‘thermodynamic’ mechanistic rationale of haloperoxidase catalysis is based on the following two assumptions: (i) the role of enzyme consists only in the rapid equilibration between the halogen-containing species originating from halide and hydrogen peroxide; (ii) the interaction between the enzyme and organic substrate is kinetically insignificant and halogenation occurs as a result of the electrophilic attack of the active brominating (Br₃ ⁻, Br₂ and HBrP) or chlorinating (HClO) species at monochlorodimedon indicative of a higher chloride ‘specificity’ of chloroperoxidase from C. fumago.

【 授权许可】

Unknown