Production of high-quality particulate methane monooxygenase in high yields from Methylococcus capsulatus (Bath) with a hollow-fiber membrane bioreactor

Journal of Bacteriology

Volumn 185, Issue 20, 2003, Pages 5915-5924

  Yu, Steve S F ^a   Chen, Kelvin H C ^a,b   Tseng, Mandy Y H ^a,b   Wang, Yane Shih ^c   Tseng, Chiu Feng ^a   Chen, Yu Ju ^a   Huang, Ded Shih ^c   Chan, Sunney I ^a  

^a INSTITUTE OF CHEMISTRY   (Taiwan)

^b NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^c NATIONAL CHENG KUNG UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ION; DUROQUINOL; METHANE MONOOXYGENASE; PROPYLENE OXIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; BACTERIAL MEMBRANE; ENZYME PURIFICATION; ENZYME SYNTHESIS; HOLLOW FIBER REACTOR; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MEMBRANE REACTOR; METHYLOCOCCUS CAPSULATUS; MICELLE; MICROENCAPSULATION; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; BIOREACTORS; CELL MEMBRANE; COPPER; CULTURE MEDIA; MEMBRANE PROTEINS; METHYLOCOCCUS CAPSULATUS; MOLECULAR SEQUENCE DATA; OXYGENASES; PEPTIDE MAPPING;

BACTERIA (MICROORGANISMS); METHYLOCOCCUS; METHYLOCOCCUS CAPSULATUS; NEGIBACTERIA;

EID: 0141960385     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.20.5915-5924.2003     Document Type: Article

References (25)

1. Anthony, C. 1982. The biochemistry of methylotrophs, p. 296-379. Academic Press, London, United Kingdom.
2. Basu, P., B. Katterle, K. K. Andersson, and H. Dalton. 2003. The membrane-associated form of methane monooxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein. Biochem. J. 369:417-427.
3. +, and CO oxidation by methanotrophs and nitrifiers. Microbiol. Rev. 53:68-84.
4. Cook S. A., and A. K. Shiemke. 1996. Evidence that copper is a required cofactor for the membrane-bound form of methane monooxygenase. J. Inorg. Chem. 63:273-284.
5. Daniel R. M., J. T. Kadonaga, R. R. Burgess, M. W. Knuth, W. A. Brennan, and S. H. Lin. 1996. Strategies for protein purification and characterization, p. 275-308. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
6. Elliott, S. J. 2000. The copper clusters of particulate methane monooxygenase: differentiation of C- and E-clusters. Ph. D. thesis. California Institute of Technology, Pasadena.
7. Finney, L. A., and T. V. O'Halloran. 2003. Transition metal speciation in the cell: insights from the chemistry of metal ion receptors. Science 300:931-936.
8. Gadd, G. M. 1990. Metal tolerance, p. 178-210. In E. Edwards (ed.), Microbiology of extreme environments. Open University Press, Milton Keynes, United Kingdom.
9. Lieberman, R. L., D. B. Sherstha, P. E. Doan, B. M. Hoffman, T. L. Stemmler, and A. C. Rosenzweig. 2003. Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster. Proc. Natl. Acad. Sci. USA 100:3820-3825.
10. Lloyd, J. S., P. D. Marco, H. Dalton, and J. C. Murrell. 1999. Heterologous expression of soluble methane monooxygenase genes in methanotrophs containing only particulate methane monooxygenase. Arch. Microbiol. 171:364-370.
11. Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
12. Malashenko, Y., I. Sokolov, and V. Romanovskaya. 2000. Role of monooxygenase reaction during assimilation of non-growth substrates by methanotrophs. J. Mol. Catal. B Enzymes 10:305-312.
13. Morton, J. D., K. F. Hayes, and J. D. Semrau. 2000. Effect of copper speciation on whole-cell soluble methane monooxygenase activity in Methylosinus trichosporium OB3b. Appl. Environ. Microbiol. 66:1730-1733.
14. Murrell, J. C., I. R. McDonald, and B. Gilbert. 2000. Regulation of expression of methane monooxygenases by copper ions. Trends Microbiol. 8:221-225.
15. Nguyen, H.-H. T., A. K. Shiemke, S. J. Jacobs, B. J. Hales, M. E. Lidstrom, and S. I. Chan. 1994. The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 269:14995-15005.
16. Nguyen, H.-H. T., K. H. Nakagawa, B. Hedman, S. J. Elliott, M. E. Lidstrom, K. O. Hodgson, and S. I. Chan. 1996. X-ray absorption and EPR studies on the copper ions associated with the particulate methane monooxygenase from Methylococcus capsulatus (Bath). Cu(I) ions and their implications. J. Am. Chem. Soc. 118:12766-12776.
17. Nguyen, H.-H. T., S. J. Elliott, J. H. Yip, and S. I. Chan. 1998. The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization. J. Biol. Chem. 273:7957-7966.
18. Prior, S. D., and H. Dalton. 1985. Acetylene as a suicide substrate and active site probe for methane monooxygenase from Methylococcus capsulatus (Bath). FEMS Microbiol. Lett. 29:105-109.
19. Prior, S. D., and H. Dalton. 1985. The effect of copper ion on membrane content and methane monooxygenase activity in methanol-grown cells of Methylococcus capsulatus (Bath). J. Gen. Microbiol. 131:155-163.
20. Semrau, J. D., A. Chistoserdov, J. Lebron, A. Costello, J. Davagnino, E. Kenna, A. J. Holmes, R. Finch, J. C. Murrel, and M. E. Lidstrom. 1995. Particulate methane monooxygenase genes in methanotrophs. J. Bacteriol. 177:3071-3079.
21. Semrau, J. D., D. Zolandz, M. E. Lidstrom, and S. I. Chan. 1995. The role of copper in the pMMO of Methylococcus capsulatus (Bath): a structural vs. catalytic function. J. Inorg. Chem. 58:235-244.
22. Shiemke, A. K., S. A. Cook, T. Miley, and P. Singleton. 1995. Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors. Arch. Biochem. Biophys. 321:421-428.
23. Takeguchi, M. K. M., and I. Okura. 1998. Purification and properties of particulate methane monooxygenase from Methylosinus trichosporium OB3b. J. Mol. Catal. A Chem. 132:145-153.
24. Xin J. Y., J. R. Cui, X. X. Hu, S. B. Li, C. G. Xia, L. M. Zhu, and Y. Q. Wang. 2002. Particulate methane monooxygenase from Methylosinus trichosporium is a copper-containing enzyme. Biochem. Biophys. Res. Commun. 295:182-186.
25. Zahn, J. A., and A. A. DiSpirito. 1996. The membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath). J. Bacteriol. 178:1018-1029.