Functional models of non-heme diiron enzymes

被引：124
作者：
Fontecave, M [1 ]
Ménage, S [1 ]
Duboc-Toia, C [1 ]
机构：
[1] Univ Grenoble 1, Lab Chim & Biochim, Ctr Redox Biol, DBMS CB CEA Grenoble EP 1087 CNRS, F-38054 Grenoble 9, France
来源：
COORDINATION CHEMISTRY REVIEWS | 1998年 / 178卷
关键词：
dioxygen activation; hydrogen peroxide; hydrolysis of phosphodiesters; methane monooxygenase; non-heme diiron complexes; ribonucleotide reductase;
D O I：
10.1016/S0010-8545(98)00119-2
中图分类号：
O61 [无机化学];
学科分类号：
070301 ; 081704 ;
摘要：
Diiron complexes are structural models of active centers of a variety of enzymes (methane monooxygenase, ribonucleotide reductase and purple acid phosphatase). More recently, they proved to have the potential to catalyze the oxidation of alkanes, alcohols, sulfides by peroxides or molecular oxygen tin the presence of electrons) and the hydrolysis of phosphodiesters. By selection of appropriate ligands, some reactions can be made highly selective, as shown from our report of the first enantioselective oxidation catalyzed by a chiral mu-oxo diiron complex. (C) 1998 Elsevier Science S.A. All rights reserved.
引用
收藏
页码：1555 / 1572
页数：18
相关论文
共 75 条
[1]  
ABERG A, 1993, BIOCHEMISTRY-US, V32, P9845
[2]  
ANDERSSON KK, 1991, NEW J CHEM, V15, P411
[3]   MECHANISM OF ASSEMBLY OF THE TYROSYL RADICAL-DIIRON(III) COFACTOR OF ESCHERICHIA-COLI RIBONUCLEOTIDE REDUCTASE .2. KINETICS OF THE EXCESS FE2+ REACTION BY OPTICAL, EPR, AND MOSSBAUER SPECTROSCOPIES [J].
BOLLINGER, JM ;
TONG, WH ;
RAVI, N ;
HUYNH, BH ;
EDMONDSON, DE ;
STUBBE, J .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1994, 116 (18) :8015-8023
[4]   Differential iron(II) affinity of the sites of the diiron cluster in protein R2 of Escherichia coli ribonucleotide reductase: Tracking the individual sites through the O-2 activation sequence [J].
Bollinger, JM ;
Chen, SX ;
Parkin, SE ;
Mangravite, LM ;
Ley, BA ;
Edmondson, DE ;
Huynh, BH .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (25) :5976-5977
[5]   BIOMIMETIC OXIDATION STUDIES .8. STRUCTURE OF A NEW MMO ACTIVE-SITE MODEL, [FE2O(H2O)2(TRIS(1-METHYLIMIDAZOL-2-YL)METHYL)AMINE)2]4+, AND ROLE OF THE AQUA LIGAND IN ALKANE FUNCTIONALIZATION REACTIONS [J].
BUCHANAN, RM ;
CHEN, S ;
RICHARDSON, JF ;
BRESSAN, M ;
FORTI, L ;
MORVILLO, A ;
FISH, RH .
INORGANIC CHEMISTRY, 1994, 33 (15) :3208-3209
[6]   Rapid freeze-quench ENDOR of the radical X intermediate of Escherichia coli ribonucleotide reductase using O-17(2), (H2O)-O-17, and (H2O)-H-2 [J].
Burdi, D ;
Sturgeon, BE ;
Tong, WH ;
Stubbe, JA ;
Hoffman, BM .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (01) :281-282
[7]   A HIGH-VALENT NONHEME IRON INTERMEDIATE - STRUCTURE AND PROPERTIES OF [FE-2(MU-O)(2)(5-ME-TPA)(2)](CLO4)(3) [J].
DONG, YH ;
FUJII, H ;
HENDRICH, MP ;
LEISING, RA ;
PAN, GF ;
RANDALL, CR ;
WILKINSON, EC ;
ZANG, Y ;
QUE, L ;
FOX, BG ;
KAUFFMANN, K ;
MUNCK, E .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1995, 117 (10) :2778-2792
[8]   Crystal structure analysis of a synthetic non-heme diiron-O-2 adduct: Insight into the mechanism of oxygen activation [J].
Dong, YH ;
Yan, SP ;
Young, VG ;
Que, L .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 1996, 35 (06) :618-620
[9]   AN EXCHANGE-COUPLED COMPLEX WITH LOCALIZED HIGH-SPIN FE-IV AND FE-III SITES OF RELEVANCE TO CLUSTER-X OF ESCHERICHIA-COLI RIBONUCLEOTIDE REDUCTASE [J].
DONG, YH ;
QUE, L ;
KAUFFMANN, K ;
MUNCK, E .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1995, 117 (45) :11377-11378
[10]   Structure of a (μ-oxo)(dihydroxo)diiron(III) complex and its reactivity toward phosphodiesters [J].
Duboc-Toia, C ;
Menage, S ;
Vincent, JM ;
Averbuch-Pouchot, MT ;
Fontecave, M .
INORGANIC CHEMISTRY, 1997, 36 (27) :6148-6149
12345678