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
[1]  
ANDERSSON KK, 1991, NEW J CHEM, V15, P411
[2]   Regiochemical variations in reactions of methylcubane with tert-butoxyl radical, cytochrome P-450 enzymes, and a methane monooxygenase system [J].
Choi, SY ;
Eaton, PE ;
Hollenberg, PF ;
Liu, KE ;
Lippard, SJ ;
Newcomb, M ;
Putt, DA ;
Upadhyaya, SP ;
Xiong, YS .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (28) :6547-6555
[3]   An agostic alternative to the P-450 rebound mechanism [J].
Collman, JP ;
Chien, AS ;
Eberspacher, TA ;
Brauman, JI .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (02) :425-426
[4]  
DALTON H, 1980, ADV APPL MICROBIOL, V26, P71
[5]   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
[6]   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
[7]  
Elango N, 1997, PROTEIN SCI, V6, P556
[8]   REACTIONS OF NONHEME IRON(II) CENTERS WITH DIOXYGEN IN BIOLOGY AND CHEMISTRY [J].
FEIG, AL ;
LIPPARD, SJ .
CHEMICAL REVIEWS, 1994, 94 (03) :759-805
[9]   HALOALKENE OXIDATION BY THE SOLUBLE METHANE MONOOXYGENASE FROM METHYLOSINUS-TRICHOSPORIUM OB3B - MECHANISTIC AND ENVIRONMENTAL IMPLICATIONS [J].
FOX, BG ;
BORNEMAN, JG ;
WACKETT, LP ;
LIPSCOMB, JD .
BIOCHEMISTRY, 1990, 29 (27) :6419-6427
[10]  
FOX BG, 1989, J BIOL CHEM, V264, P10023