High-valent iron in chemical and biological oxidations

被引:502
作者
Groves, John T. [1 ]
机构
[1] Princeton Univ, Dept Chem, Princeton, NJ 08544 USA
关键词
cytochrome P450; chloroperoxidase; AlkB; sMMO; oxygen rebound; ferryl; Fenton; mechanism;
D O I
10.1016/j.jinorgbio.2006.01.012
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Various aspects of the reactivity of iron(IV) in chemical and biological systems are reviewed. Accumulated evidence shows that the ferryl species [Fe(IV)=O](2+) can be formed under a variety of conditions including those related to the ferrous ion-hydrogen peroxide system known as Fenton's reagent. Early evidence that such a species could hydroxylate typical aliphatic C-H bonds included regioselectivities and stereospecificities for cyclohexanol hydroxylation that could not be accounted for by a freely diffusing hydroxyl radical. Iron(lV) porphyrin complexes are also found in the catalytic cycles of cytochrome P450 and chloroperoxidase. Model oxo-iron(IV) porphyrin complexes have shown reactivity similar to the proposed enzymatic intermediates. Mechanistic studies using mechanistically diagnostic substrates have implicated a radical rebound scenario for aliphatic hydroxylation by cytochrome P450. Likewise, several non-heme diiron hydroxylases, AlkB (Q-hydroxylase), sMMO (soluble methane monooxygenase), XyIM (xylene monooxygenase) and T4moH (toluene monooxygenase) all show clear indications of radical rearranged products indicating that the oxygen rebound pathway is a ubiquitous mechanism for hydrocarbon oxygenation by both heme and non-heme iron enzymes. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:434 / 447
页数:14
相关论文
共 115 条
[51]   COMPOUND-I AND COMPOUND-II ANALOGS OF A CHLORIN [J].
JAYARAJ, K ;
GOLD, A ;
AUSTIN, RN ;
MANDON, D ;
WEISS, R ;
TERNER, J ;
BILL, E ;
MUTHER, M ;
TRAUTWEIN, AX .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1995, 117 (35) :9079-9080
[52]   Compound I and compound II analogues from porpholactones [J].
Jayaraj, K ;
Gold, A ;
Austin, RN ;
Ball, LM ;
Terner, J ;
Mandon, D ;
Weiss, R ;
Fischer, J ;
DeCian, A ;
Bill, E ;
Muther, M ;
Schunemann, V ;
Trautwein, AX .
INORGANIC CHEMISTRY, 1997, 36 (20) :4555-4566
[53]   Influence of meso substituents on electronic states of (oxoferryl)porphyrin pi-cation radicals [J].
Jayaraj, K ;
Terner, J ;
Gold, A ;
Roberts, DA ;
Austin, RN ;
Mandon, D ;
Weiss, R ;
Bill, E ;
Muther, M ;
Trautwein, AX .
INORGANIC CHEMISTRY, 1996, 35 (06) :1632-1640
[54]   High-valent nonheme iron.: Two distinct iron(IV) species derived from a common iron(II) precursor [J].
Jensen, MP ;
Costas, M ;
Ho, RYN ;
Kaizer, J ;
Payeras, AMI ;
Münck, E ;
Que, L ;
Rohde, JU ;
Stubna, A .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (30) :10512-10525
[55]   Radical intermediates in the catalytic oxidation of hydrocarbons by bacterial and human cytochrome P450 enzymes [J].
Jiang, YY ;
He, X ;
de Montellano, PRO .
BIOCHEMISTRY, 2006, 45 (02) :533-542
[56]  
Jin N, 2000, ANGEW CHEM INT EDIT, V39, P3849, DOI 10.1002/1521-3773(20001103)39:21<3849::AID-ANIE3849>3.0.CO
[57]  
2-0
[58]   Unusual kinetic stability of a ground-state singlet oxomanganese(V) porphyrin. Evidence for a spin state crossing effect [J].
Jin, N ;
Groves, JT .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (12) :2923-2924
[59]   Soluble methane monooxygenase: activation of dioxygen and methane [J].
Kopp, DA ;
Lippard, SJ .
CURRENT OPINION IN CHEMICAL BIOLOGY, 2002, 6 (05) :568-576
[60]   THE CENTENNIAL OF THE FENTON REACTION [J].
KOPPENOL, WH .
FREE RADICAL BIOLOGY AND MEDICINE, 1993, 15 (06) :645-651