A MIXED-VALENT, UNSYMMETRICAL (FEFEIII)-FE-II COMPLEX WITH A TERMINAL PHENOLATO LIGAND AS A MODEL FOR THE ACTIVE-SITE OF PURPLE ACID-PHOSPHATASES

被引：46
作者：
BERNARD, E
MONETA, W
LAUGIER, J
CHARDONNOBLAT, S
DERONZIER, A
TUCHAGUES, JP
LATOUR, JM
机构：
[1] CENG, DEPT RECH FONDAMENTALE MAT CONDENSEE, CHIM COORDINAT LAB, F-38041 GRENOBLE, FRANCE
[2] CENG, DEPT RECH FONDAMENTALE MAT CONDENSEE, STRUCT LAB, GRENOBLE, FRANCE
[3] UNIV GRENOBLE 1, ELECTROCHIM ORGAN & PHOTOCHIM REDOX LAB, GRENOBLE, FRANCE
[4] CNRS, CHIM COORDINAT LAB, F-31077 TOULOUSE, FRANCE
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 1994年 / 33卷 / 08期
关键词：
D O I：
10.1002/anie.199408871
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The structure and the magnetic and electrochemical properties of the active center of purple acid phosphatases are modeled by a complex that mimics the terminal coordination of the tyrosine residue and was prepared with a new heptadentate phenola‐to ligand system. The instability of the reduced FeIIFeII state of the enzyme may be attributed to the terminal ligand, since the phenolato ligand in the model is a destabilizing factor. Copyright © 1994 by VCH Verlagsgesellschaft mbH, Germany
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页码：887 / 889
页数：3
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