Domain Engineering of the Reductase Component of Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath)

Journal of Biological Chemistry

Volumn 279, Issue 7, 2004, Pages 5630-5640

  Blazyk, Jessica L ^a   Lippard, Stephen J ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ELECTRON TRANSPORT PROPERTIES; ENZYMES; METHANE; METHANOL; REDOX REACTIONS; SPECTROSCOPIC ANALYSIS;

ELECTRON TRANSFER RATES; THREE COMPONENT ENZYME SYSTEMS;

BIOCHEMISTRY;

FERREDOXIN; FLAVINE ADENINE NUCLEOTIDE; METHANE; METHANE MONOOXYGENASE; METHANOL; OXIDOREDUCTASE; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SOLVENT;

ARTICLE; CATALYSIS; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME REGULATION; HYDROXYLATION; METHYLOCOCCUS CAPSULATUS; NONHUMAN; OPTICS; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN ENGINEERING; STEADY STATE;

CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DNA; ELECTRON TRANSPORT; ELECTRONS; FLAVINS; GENETIC VECTORS; HYDROGEN-ION CONCENTRATION; KINETICS; METHYLOCOCCUS CAPSULATUS; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; OXYGEN; OXYGENASES; PLASMIDS; PROTEIN STRUCTURE, TERTIARY; SPECTROPHOTOMETRY; TEMPERATURE; ULTRAVIOLET RAYS;

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

EID: 1242317007     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M308940200     Document Type: Article

References (41)

1. Higgins, I. J., Best, D. J., Hammond, R. C., and Scott, D. (1981) Microbiol. Rev. 45, 556-590
2. Hanson, R. S., and Hanson, T. E. (1996) Microbiol. Rev. 60, 439-471
3. Prior, S. D., and Dalton, H. (1985) J. Gen. Microbiol. 131, 155-163
4. Murrell, J. C. (1994) Biodegradation 5, 145-159
5. Nguyen, H.-H. T., Elliott, S. J., Yip, J. H.-K., and Chan, S. I. (1998) J. Biol. Chem. 273, 7957-7966
6. Lieberman, R. L., Shrestha, D. B., Doan, P. E., Hoffman, B. M., Stemmler, T. L., and Rosenzweig, A. C. (2003) Proc. Natl. Acad. Sci. U. S.A. 100, 3820-3825
7. Colby, J., and Dalton, H. (1978) Biochem. J. 171, 461-468
8. Pilkington, S. J., and Dalton, H. (1990) Methods Enzymol. 188, 181-190
9. Fox, B. G., Froland, W. A., Dege, J. E., and Lipscomb, J. D. (1989) J. Biol. Chem. 264, 10023-10033
10. Fox, B. G., Froland, W. A., Jollie, D. R., and Lipscomb, J. D. (1990) Methods Enzymol. 188, 191-202
11. Woodland, M. P., and Dalton, H. (1984) J. Biol. Chem. 259, 53-59
12. Feig, A. L., and Lippard, S. J. (1994) Chem. Rev. 94, 759-805
13. Liu, K. E., and Lippard, S. J. (1995) in Adv. Inorg. Chem. (Sykes, A. G., ed) Vol. 42, pp. 263-289, Academic Press, San Diego
14. Wallar, B. J., and Lipscomb, J. D. (1996) Chem. Rev. 96, 2625-2657
15. Valentine, A. M., and Lippard, S. J. (1997) Dalton Trans. 21, 3925-3931
16. Gassner, G. T., and Lippard, S. J. (1999) Biochemistry 38, 12768-12785
17. Solomon, E. I., Brunold, T. C., Davis, M. I., Kemsley, J. N., Lee, S.-K., Lehnert, N., Neese, F., Skulan, A. J., Yang, Y.-S., and Zhou, J. (2000) Chem. Rev. 100, 235-349
18. Merkx, M., Kopp, D. A., Sazinsky, M. H., Blazyk, J. L., Müller, J., and Lippard, S. J. (2001) Angew. Chem. Int. Ed. 40, 2782-2807
19. Whittington, D. A., and Lippard, S. J. (2001) in Handbook of Metalloproteins (Messerschmidt, A., Huber, R., Poulos, T., and Wieghardt, K., eds) pp. 712-724, Wiley, Chichester
20. Stainthorpe, A. C., Lees, V., Salmond, G. P. C., Dalton, H., and Murrell, J. C. (1990) Gene (Amst.) 91, 27-34
21. Colby, J., and Dalton, H. (1979) Biochem. J. 177, 903-908
22. Lund, J., and Dalton, H. (1985) Eur. J. Biochem. 147, 291-296
23. Fox, B. G., Hendrich, M. P., Surerus, K. K., Andersson, K. K., Froland, W. A., Lipscomb, J. D., and Münck, E. (1993) J. Am. Chem. Soc. 115, 3688-3701
24. Kopp, D. A., Gassner, G. T., Blazyk, J. L., and Lippard, S. J. (2001) Biochemistry 40, 14932-14941
25. Müller, J., Lugovskoy, A. A., Wagner, G., and Lippard, S. J. (2002) Biochemistry 41, 42-51
26. Lund, J., Woodland, M. P., and Dalton, H. (1985) Eur. J. Biochem. 147, 297-305
27. Green, J., and Dalton, H. (1989) Biochem. J. 259, 167-172
28. Andrews, S. C., Shipley, D., Keen, J. N., Findlay, J. B. C., Harrison, P. M., and Guest, J. R. (1992) FEBS Lett. 302, 247-252
29. Karplus, P. A., Daniels, M. J., and Herriott, J. R. (1991) Science 251, 60-66
30. Correll, C. C., Batie, C. J., Ballou, D. P., and Ludwig, M. L. (1992) Science 258, 1604-1610
31. Blazyk, J. L., and Lippard, S. J. (2002) Biochemistry 41, 15780-15794
32. Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) Nucleic Acids Res, 22, 4673-4680
33. Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997) Nucleic Acids Res. 25, 3389-3402
34. Crasto, C. J., and Feng, J. (2000) Prot. Eng. 13, 309-312
35. Stainthorpe, A. C., Murrell, J. C., Salmond, G. P. C., Dalton, H., and Lees, V. (1989) Arch. Microbiol. 152, 154-159
36. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
37. Massey, V. (1957) J. Biol. Chem. 229, 763-770
38. Stookey, L. L. (1970) Anal. Chem. 42, 779-781
39. Coufal, D. E., Blazyk, J. L., Whittington, D. A., Wu, W. W., Rosenzweig, A. C., and Lippard, S. J. (2000) Eur. J. Biochem. 267, 2174-2185
40. Kurisu, G., Kusunoki, M., Katoh, E., Yamazaki, T., Teshima, K., Onda, Y., Kimata-Ariga, Y., and Hase, T. (2001) Nat. Struct. Biol. 8, 117-121
41. Karlsson, A., Beharry, Z. M., Eby, D. M., Coulter, E. D., Neidle, E. L., Kurtz, D. M., Jr., Eklund, H., and Ramaswamy, S. (2002) J. Mol. Biol. 318, 261-272