A Biomimetic System for Studying Salicylate Dioxygenase.
A Biomimetic System for Studying Salicylate Dioxygenase.
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用于研究水杨酸双加氧酶的仿生系统。
DOI:
10.1021/bk-2019-1317.ch004
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发表时间:
2019
期刊:
影响因子:
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通讯作者:
Chavez,FermanA
中科院分区:
文献类型:
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作者:
Banerjee,Atanu;Li,Jia;Molenda,MonikaA;Brennessel,WilliamW;Chavez,FermanA
We report the characterization of [Fe(T1Et4iPrIP)(sal)] (2) (T1Et4iPrIP = tris(1-ethyl-4-isopropyl-imidazolyl)phosphine; sal2–= salicylate dianion), which serves as a model for substrate-bound salicylate dioxygenase (SDO). Complex2crystallizes in the monoclinic space groupP21/n witha= 10.7853(12) Å,b= 16.5060(19) Å,c= 21.217(2) Å,β= 94.489(2)°,andV= 3765.5(7) Å3. The structure consists of FeIIbonded in distorted square pyramidal geometry (τ= 0.32) with two salicylate oxygens and two T1Et4iPrIP nitrogens serving as the base and the apical position occupied by the other ligand nitrogen. [Fe(T1Et4iPrIP)(OTf)2] (1), the precursor for2, catalyzes the cleavage of 1,4-dihydroxy-2-naphthoate in the presence of O2. Complex1is also capable of cleaving the salicylate aromatic ring in the presence of H2O2. The progression of this reaction toward product formation involves an FeIII–phenoxide species.