Dioxygen oxidation of hydrocarbons by a methane monooxygenase-like system: Diiron complex-O2-Zn/HOAc-MV2+

Science in China, Series B: Chemistry

Volumn 42, Issue 2, 1999, Pages 131-137

  Wei, Junfa ^a   He, Diping ^a   Yu, Xianda ^b  

^a SHAANXI NORMAL UNIVERSITY   (China)

^b LANZHOU INSTITUTE OF CHEMICAL PHYSICS   (China)

Author keywords

Biomimetic catalysis; Diiron complex; Dioxygen activation; Methane monooxygenase; Model system; Selective oxidation

Indexed keywords

EID: 0343846788     PISSN: 10069291     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02875508     Document Type: Article

References (16)

1. Anthony, C., The Biochemistry of Methylotrophs, New York: Academic Press, 1982, 296-379.
2. Fox, B. G., Borneman, J. G., Wackett, L. P. et al., Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: mechanistic and environmental implications, Biochemistry, 1990, 29: 6419.
3. Green, J., Dalton, H., The biosynthesis and assembly of protein A of soluble methane monooxygenase of Methylococcus capsulatus (Bath), J. Biol. Chem., 1989, 264: 17698.
4. Wei, J. F., Yu, X. D., Jin, D. S., Progress in the research on monooxygenases with dinuclear centre and their model systems (in Chinese), Progress in Chemistry, 1994, 6(9): 178.
5. Feig, A. L., Lippard, S. J., Reactions of non-heme iront (II) centers with dioxygen in biology and chemistry, Chem. Rev., 1994, 94: 759.
6. Liu, K. E., Valentine, A. M., Wang, D. et al., Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath), J. Am. Chem. Soc., 1995, 117: 1074.
7. Dalton, H., Biological methane activation: lesson for the chemists, Catal. Today, 1992, 13: 455.
8. Que, L. Jr., Ture, A. E., Dinuclear iron and manganase-oxo sites in biology, Prog. Inorg. Chem., 1990, 38: 97.
9. Kitajima, N., Fukui, H., Morooka, Y., A model for methane monooxygenase: dioxygen oxidation of alkanes by use of a μ-oxo binuclear iron complex, J. Chem. Soc., Chem. Commun., 1988, (7): 485.
10. Yoon, H., Burrows, C. J., Catalysis of alkene oxidation by nickel(II) salen complexes using sodium hyperchlorite under phase transfer conditions, J. Am. Chem. Soc., 1988, 110: 4087.
11. Wang, K., Bioinorganic Chemistry, Beijing: Qinghua University Press, 1988, 107-108.
12. Fox, B. G., Surerus, K. K., Munck, E. et al., Evidence for a μ-oxo-bridged binuclear iron cluster in the hydroxylase component of methane monooxygenase: Mossbauer and EPR studies, J. Bio. Chem., 1988, 263: 10553.
13. Fox, B. G., Froland, W. A., Dege, J. E. et al., Methane monooxygenase from Methylosinus trichosporium OB3b, Purification and properties of a three-component system with high specific activity from a type II methanotroph, J. Bio. Chem., 1989, 264: 10023.
14. Liu, K. E., Johnson, C. C., Newcomb, M. et al., Radical clock substrate probes and kinetic isotope effect studies of the hydroxylation of hydrocarbons by methane monooxygenase, J. Am. Chem. Soc., 1993, 115: 939.
15. Calderwood, T. S., Bruìce, T. C., Spectral and electrochemical identification of iron (IV)-oxo porphyrin and iron (V)-oxo-porphyrin π-cation species, J. Am. Chem. Soc., 1995, 107: 8272.
16. Rosenzweig, A. C-, Friderick, C. A., Lippard, S. J., Crystal structure of a bacterical non-heme iron hydroxylase that catalyzes the biological oxidation of methane, Nature, 1993, 366: 537.