Structural models of vanadate-dependent haloperoxidases and their reactivity

Journal of Chemical Sciences

Mannar R Maurya1¹ 

[1] Department of Chemistry, Indian Institute of Technology, Roorkee 247 667$$

关键词: Structural models;    haloperoxidases;    vanadium complexes;    reactivity of vanadium complexes.;   

DOI  :  

来源: Indian Academy of Sciences

【 摘 要 】

Vanadium(V) complexes with hydrazone-based ONO and ONN donor ligands that partly model active-site structures of vanadate-dependent haloperoxidases have been reported. On reaction with [VO(acac)2] (Hacac = acetylacetone) under nitrogen, these ligands generally provide oxovanadium(IV) complexes [VO(ONO)X] (X = solvent or nothing) and [VO(acac)(ONN)], respectively. Under aerobic conditions, these oxovanadium(IV) species undergo oxidation to give oxovanadium(V), dioxovanadium (V) or 𝜇-oxobis{oxovanadium(V)} species depending upon the nature of the ligand. Anionic and neutral dioxovanadium(V) complexes slowly deoxygenate in methanol to give monooxo complexes [VO(OMe)(MeOH)(ONO)]. The anionic complexes [VO2(ONO)]- can also be converted in situ on acidification to oxohydroxo complexes [VO(OH)(HONO)]+ and to peroxo complexes [VO(O2)(ONO)]-, and thus to the species assumed to be intermediates in the haloperoxidases activity of the enzymes. In the presence of catechol (H2cat) and benzohydroxamic acid (H2bha), oxovanadium (IV) complexes, [VO (acac)(ONN)] gave mixed-chelate oxovanadium(V) complexes [VO(cat)(ONN)] and [VO(bha)(ONN)] respectively. These complexes are not very stable in solution and slowly convert to the corresponding dioxo species [VO2(ONN)] as observed by 51V NMR and electronic absorption spectroscopic studies.

【 授权许可】

Unknown