參考文獻 |
1. Higgins, I. J.; Best, D. J.; Hammond, R. C., New findings in methane-utilizing
bacteria highlight their importance in the biosphere and their commercial potential.
Nature 1980, 286, (5773), 561-564.
2. Finkelstein, J., Structural biology: methanol maker. Nature 2005, 434, (7030), 151.
3. Murrell, J.C.; Gilbert, B.; McDonald, I.R.; Molecular biology and regulation of methane monoxygenase. Arch Microbiol 2000 173:325-332
4. Hanson, R. S.; Hanson, T. E., Methanotrophic bacteria. Microbiol Rev 1996, 60,
(2), 439-71.
5. Semrau, J. D.; Zolandz, D.; Lindstrom, M. E.; Chan, S. I., The role of copper in the
pMMO of Methylococcus capsulatus Bath: A structural vs. catalytic function.
Journal of Inorganic Biochemistry 1995, 58, (4), 235-244.
6. Rosenzweig, A. C.; Frederick, C. A.; Lippard, S. J.; Nordlund, P.; auml, Crystal
structure of a bacterial non-haem iron hydroxylase that catalyses the biological
oxidation of methane. Nature 1993, 366, (6455), 537-543.
7. Basu, P.; Katterle, B.; Andersson, K. K.; Dalton, H., The membrane-associated
form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a
copper/iron protein. Biochem J 2003, 369, (Pt 2), 417-27.
8. Lieberman, R. L.; Shrestha, D. B.; Doan, P. E.; Hoffman, B. M.; Stemmler, T. L.;
Rosenzweig, A. C., Purified particulate methane monooxygenase from
Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a
copper-containing cluster. Proc Natl Acad Sci U S A 2003, 100, (7), 3820-5.
9. Lieberman, R. L.; Rosenzweig, A. C., Crystal structure of a membrane-bound
metalloenzyme that catalyses the biological oxidation of methane. Nature 2005,
434, (7030), 177-82.
10. Takeguchi, M.; Miyakawa, K.; Okura, I., The role of copper in particulate methane
monooxygenase from Methylosinus trichosporium OB3b. Journal of Molecular
Catalysis A: Chemical 1999, 137, (1-3), 161-168.
11. Semrau, J. D.; Chistoserdov, A.; Lebron, J.; Costello, A.; Davagnino, J.; Kenna, E.;
Holmes, A. J.; Finch, R.; Murrell, J. C.; Lidstrom, M. E., Particulate methane
monooxygenase genes in methanotrophs. J Bacteriol. 1995, 177, (11), 3071-3079.
12. Hakemian, A.S.; Rosenzweig, A.C., The biochemistry of methane oxidation.
Annu Rev Biochem. 2007, 76, 223-241
13. Lienerman, R.L.; Rosenzweig, A.C., Biological methane oxidation: reduction, biochemistry, and active site structure of particulate methane monooxygenase.
Crit. Rev. Biochem Mol Biol. 2004, 39(3) 147-164.
14. Nguyen, H. H.; Elliott, S. J.; Yip, J. H.; Chan, S. I., The particulate methane
monooxygenase from methylococcus capsulatus (Bath) is a novel
copper-containing three-subunit enzyme. Isolation and characterization. J Biol
Chem 1998, 273, (14), 7957-66.
15. Yu, S. S.; Chen, K. H.; Tseng, M. Y.; Wang, Y. S.; Tseng, C. F.; Chen, Y. J.;Huang, D. S.; Chan, S. I., Production of high-quality particulate methane monooxygenase in high yields from Methylococcus capsulatus (bath) with a hollow-fiber membrane bioreactor. J Bacteriol 2003, 185, (20), 5915-24.
16. Chan, S. I.; Chen, K. H.; Yu, S. S.; Chen, C. L.; Kuo, S. S., Toward delineating the
structure and function of the particulate methane monooxygenase from
methanotrophic bacteria. Biochemistry 2004, 43, (15), 4421-30.
17. Vinchurkar, M. S.; Chen, K. H.; Yu, S. S.; Kuo, S. J.; Chiu, H. C.; Chien, S. H.;
Chan, S. I., Polarized ATR-FTIR spectroscopy of the membrane-embedded
domains of the particulate methane monooxygenase. Biochemistry 2004, 43, (42),
13283-92.
18. Yu, S.S.; Ji, C.Z.; Wu, Y.P.; Lee, T.L.; Lai, C.H.; Lin, S.C.; Yang, Z.L.; Wang, V.C.; Chen, K.H.; Chan, S.I., The C-terminal aqueous-exposed domain of the 45kDa subunit of the particulate methane monoxygenase in Methylcoccus capsulatus (Bath) is a Cu(I) sponge. Biochemistry 2007, 46, 13762-13774
19. Chan, S.I.; Wang, V.C.; Lai, J.C.; Yu, S.S.; Chen, P.P.; Chen, K.H.; Chen, C.L.; Chan, M.K., Redox potentiometry studies of particulate methane monoxygenase support for a trinuclear copper cluster active site. Angew. Chem. Int. Ed. 2007, 46, 1992-1994
20.Chen, P.P.; Yang, R.B.; Lee, J.C.; Chan, S.I., Facile O-atom insertion into C-C and C-H bonds by a trinuclear copper complex designed to harness a singlet oxene. Proc. Natl. Acad. Sci. U.S.A. 2007, 104(37):14570-14575
21. Chen, P.P.; Chan, S.I., Theoretical modeling of the hydroxylation of methane as mediated by the particulate methane monooxygenase. J Inorg Biochem. 2006 100(4) 801-809
22. Yu, S.S.; Wu, L.Y.; Chen, K.H.; Luo, W.I.; Huang, D.S.; Chan, S.I., The stereospecific hydroxylation of [2,2-2H2]butane and chiral dideuteriobutanes by the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J Biol Chem. 2003 278(42) 40658-40669
23. Huang, D.S.; Wu, S.H.; Wang, Y.S.; Yu S.S.; Chan S.I., Determination of the carbon kinetic isotope effects on propane hydroxylation mediated by the methane monooxygenases from Methylococcus capsulatus (Bath) by using stable carbon isotopic analysis. Chembiochem. 2002 3(8) 760-765
24. Chen, C.L.; Chen, K.H.; Ke, S.C.; Yu, S.S.; Chan, S.I., Preparation and characterization of a (Cu, Zn)-pMMO from Methylcoccus capsulatus (Bath). Journal of Inorganic Biochemistry 98(2004) 2125-2130
25. Ng, K.Y.; Yu, S.S.; Chan, S.I., unpublished data, 2008
26. Rosen, B.P., Transport and detoxification systems for transition metals, heavy
metals and metalloids in eukaryotic and prokaryotic microbes. Comparative Biochemistry and Physiology Part A 133 (2002) 689–693
27. Resing, C.; Grass, G. Escherichia coli mechanisms of copper homeostasis in
a changing environment. FEMS Microbiology Reviews 27 (2003) 197-213
28. KrÓliczewski, J.; Szczepaniak, A., In vitro reconstitution of the spinach chloroplast cytochrome b6 protein from a fusion protein expressed in Escherichia coli. Biochimica et Biophysica Acta 1598(2002) 177-184
29 Smyth, D.R.; Mrozkiewicz, M.K.; McGrath, W.J.; Listwan, P.; Kobe, B., Crystal structures of fusion proteins with large-affinity tags. Protein Science 2003 July;12(7) 1313-22
30. Arechaga, I.; Miroux, B.; Karrasch, S.; Huijbregts, R.; Kruiift, B.D.; Runswick, M.J. ; Walker, J.E., Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F1F0 ATP synthase. FEBS letters 482(2000) 215-219
31. 王琢堅, Implications of the redox behavior of the copper clusters in the particulate
methane monooxygenase on the methane hydroxylation mechanism. 國立台灣大學化學研究所碩士論文, 2005.
32. 林素卿, Reconstitution of membrane proteins or subunits for structural and functional studies. 國立台灣大學化學研究所博士論文, 2007
33. 楊秉恭, Models for the trinuclear copper clusters of the particulate methane monoxygenase from nethanotrophic bacteria: synthesis, spectroscopic characterization of trinuclear copper complexes. 國立中央大學化學研究所碩士論文, 2006
34. 陳家全 李家維 楊瑞森, 生物電子顯微鏡學 行政院國家科學委員會精密儀器發展中心編印, 1991 |