MMO: P450 in wolf's clothing?

被引:61
作者
Lipscomb, JD
Que, L
机构
[1] Univ Minnesota, Dept Biochem, Minneapolis, MN 55455 USA
[2] Univ Minnesota, Dept Chem, Minneapolis, MN 55455 USA
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 1998年 / 3卷 / 03期
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
monooxygenase mechanism; oxygen activation; Fe(IV); compound Q; model complexes;
D O I
10.1007/s007750050241
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
Methane monooxygenase (MMO) catalyzes the oxidation of stable hydrocarbons that are :not attacked by cytochrome P450 monooxygenase. A key transient intermediate in the catalytic cycle of the soluble form of MMO termed compound Q (Q) has been trapped and characterized through spectroscopic comparisons with novel high valent model complexes. Q appears to contain a non-heme dinuclear Fe(IV) cluster bridged by at least two single oxygen atoms to form a so-called diamond core. Q has the ability to react directly with unactivated hydrocarbons to yield oxidized products, Several types of experiments indicate that this reaction involves formation of an intermediate, probably with radical character. This is consistent with a hydrogen atom abstraction mechanism analogous to that ascribed to cytochrome P450. However, these same experiments show that a pure hydrogen atom abstraction mechanism is unlikely for many substrates without an additional interaction between the intermediate that is formed and the high valent cluster. The results may be of general relevance to monooxygenase catalysis.
引用
收藏
页码:331 / 336
页数:6
相关论文
共 40 条
[21]   RADICAL CLOCK SUBSTRATE PROBES AND KINETIC ISOTOPE EFFECT STUDIES OF THE HYDROXYLATION OF HYDROCARBONS BY METHANE MONOOXYGENASE [J].
LIU, KE ;
JOHNSON, CC ;
NEWCOMB, M ;
LIPPARD, SJ .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1993, 115 (03) :939-947
[22]   GATING EFFECTS OF COMPONENT-B ON OXYGEN ACTIVATION BY THE METHANE MONOOXYGENASE HYDROXYLASE COMPONENT [J].
LIU, Y ;
NESHEIM, JC ;
LEE, SK ;
LIPSCOMB, JD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (42) :24662-24665
[23]   Structural, spectroscopic, and theoretical characterization of bis(mu-oxo)dicopper complexes, novel intermediates in copper-mediated dioxygen activation [J].
Mahapatra, S ;
Halfen, JA ;
Wilkinson, EC ;
Pan, GF ;
Wang, XD ;
Young, VG ;
Cramer, CJ ;
Que, L ;
Tolman, WB .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (46) :11555-11574
[24]  
McMurry T.J., 1986, CYTOCHROME P450 STRU, P1
[25]   Large kinetic isotope effects in methane oxidation catalyzed by methane monooxygenase: Evidence for C-H bond cleavage in a reaction cycle intermediate [J].
Nesheim, JC ;
Lipscomb, JD .
BIOCHEMISTRY, 1996, 35 (31) :10240-10247
[26]   STRUCTURAL CHARACTERIZATION OF HORSERADISH-PEROXIDASE USING EXAFS SPECTROSCOPY - EVIDENCE FOR FE=O LIGATION IN COMPOUND-I AND COMPOUND-II [J].
PENNERHAHN, JE ;
EBLE, KS ;
MCMURRY, TJ ;
RENNER, M ;
BALCH, AL ;
GROVES, JT ;
DAWSON, JH ;
HODGSON, KO .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1986, 108 (24) :7819-7825
[27]   CRYPTIC STEREOSPECIFICITY OF METHANE MONOOXYGENASE [J].
PRIESTLEY, ND ;
FLOSS, HG ;
FROLAND, WA ;
LIPSCOMB, JD ;
WILLIAMS, PG ;
MORIMOTO, H .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1992, 114 (19) :7561-7562
[28]   Modeling the oxygen activation chemistry of methane monooxygenase and ribonucleotide reductase [J].
Que, L ;
Dong, YH .
ACCOUNTS OF CHEMICAL RESEARCH, 1996, 29 (04) :190-196
[29]  
ROSENZWEIG AC, 1993, NATURE, V366, P537, DOI 10.1038/366537a0
[30]   GEOMETRY OF THE SOLUBLE METHANE MONOOXYGENASE CATALYTIC DIIRON CENTER IN 2 OXIDATION-STATES [J].
ROSENZWEIG, AC ;
NORDLUND, P ;
TAKAHARA, PM ;
FREDERICK, CA ;
LIPPARD, SJ .
CHEMISTRY & BIOLOGY, 1995, 2 (06) :409-418