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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