Expression and characterization of ferredoxin and flavin adenine dinucleotide binding domains of the reductase component of soluble methane monooxygenase from Methylococcus capsulatus (Bath)

Biochemistry

Volumn 41, Issue 52, 2002, Pages 15780-15794

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

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FLAVIN COFACTOR;

BACTERIA; CATALYSIS; ELECTRIC POTENTIAL; METHANE; METHANOL; OXIDATION; REACTION KINETICS; SPECTROSCOPIC ANALYSIS;

ENZYMES;

FERREDOXIN; FLAVINE ADENINE NUCLEOTIDE; HYDROQUINONE; METHANE; METHANE MONOOXYGENASE; METHANOL; OXIDOREDUCTASE; OXYGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SEMIQUINONE;

ARTICLE; CATABOLISM; CATALYSIS; CHEMICAL REACTION; CHEMICAL REACTION KINETICS; CHEMICAL STRUCTURE; ELECTRON TRANSPORT; ESCHERICHIA COLI; KINETICS; METHANOTROPHIC BACTERIUM; METHYLOCOCCUS CAPSULATUS; OXIDATION; OXIDATION REDUCTION POTENTIAL; PH; PKA; PRIORITY JOURNAL; PROTEIN EXPRESSION; ULTRAVIOLET SPECTROSCOPY;

BINDING SITES; CLONING, MOLECULAR; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT; FERREDOXIN-NADP REDUCTASE; FERREDOXINS; FLAVIN-ADENINE DINUCLEOTIDE; KINETICS; METHYLOCOCCUS CAPSULATUS; NAD; OXIDATION-REDUCTION; OXYGENASES; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SOLUBILITY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROPHOTOMETRY, ULTRAVIOLET;

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

EID: 0037207140     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026757f     Document Type: Article

References (43)

1. Higgins, I. J., Best, D. J., and Hammond, R. C. (1980) New findings in methane-utilizing bacteria highlight their importance in the biosphere and their commercial potential, Nature 286, 561-564.
2. Nguyen, H.-H. T., Elliott, S. J., Yip, J. H.-K., and Chan, S. I. (1998) The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme, J. Biol. Chem. 273, 7957-7966.
3. Prior, S. D., and Dalton, H. (1985) The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells of Methylococcus capsulatus (Bath), J. Gen. Microbiol. 131, 155-163.
4. Woodland, M. P., and Dalton, H. (1984) Purification and characterization of component A of the methane monooxygenase from Methylococcus capsulatus (Bath), J. Biol. Chem. 259, 53-59.
5. Green, J., and Dalton, H. (1985) Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath), J. Biol. Chem. 260, 15795-15801.
6. Liu, K. E., and Lippard, S. J. (1995) Studies of the Soluble Methane Monooxygenase Protein System: Structure, Component Interactions, and Hydroxylation Mechanism, in Advances in Inorganic Chemistry (Sykes, A. G., Ed.) pp 263-289, Academic Press, San Diego.
7. Feig, A. L., and Lippard, S. J. (1994) Reactions of non-heme iron-(II) centers with dioxygen in biology and chemistry, Chem. Rev. 94, 759-805.
8. Wallar, B. J., and Lipscomb, J. D. (1996) Dioxygen activation by enzymes containing binuclear non-heme iron clusters, Chem. Rev. 96, 2625-2657.
9. Merkx, M., Kopp, D. A., Sazinsky, M. H., Blazyk, J. L., Müller, J., and Lippard, S. J. (2001) Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: a tale of two irons and three proteins, Angew. Chem., Int. Ed. 40, 2782-2807.
10. Colby, J., and Dalton, H. (1978) Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components, Biochem. J. 171, 461-468.
11. Gassner, G. T., and Lippard, S. J. (1999) Component interactions in the soluble methane monooxygenase system from Methylococcus capsulatus (Bath), Biochemistry 38, 12768-12785.
12. Merkx, M., and Lippard, S. J. (2002) Why OrfY? Characterization of MMOD, a long-overlooked component of the soluble methane monooxygenase from Methylococcus capsulatus (Bath), J. Biol. Chem. 277, 5858-5865.
13. 2 redox centres of component C, the NADH:acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath), Eur. J. Biochem. 147, 291-296.
14. Lund, J., Woodland, M. P., and Dalton, H. (1985) Electron-transfer reactions in the soluble methane monooxygenase of Methylococcus capsulatus (Bath), Eur. J. Biochem. 147, 297-305.
15. Stainthorpe, A. C., Lees, V., Salmond, G. P. C., Dalton, H., and Murrell, J. C. (1990) The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath), Gene 91, 27-34.
16. Kopp, D. A., Gassner, G. T., Blazyk, J. L., and Lippard, S. J. (2001) Electron-transfer reactions of the reductase component of soluble methane monooxygenase from Methylococcus capsulatus (Bath), Biochemistry 40, 14932-14941.
17. + reductases, FEBS Lett. 302, 247-252.
18. + reductase: prototype for a structurally novel flavoenzyme family, Science 251, 60-66.
19. Correll, C. C., Batie, C. J., Ballou, D. P., and Ludwig, M. L. (1992) Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S], Science 258, 1604-1610.
20. Gassner, G. T., and Ballou, D. P. (1995) Preparation and characterization of a truncated form of phthalate dioxygenase reductase that lacks an iron-sulfur domain, Biochemistry 34, 13460-13471.
21. Massey, V. (1957) Studies on succinic dehydrogenase. VII. Valency state of the iron in beef heart succinic dehydrogenase, J. Biol. Chem. 229, 763-770.
22. Stookey, L. L. (1970) Ferrozine: a new spectrophotometric reagent for iron, Anal. Chem. 42, 779-781.
23. Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22, 4673-4680.
24. Stainthorpe, A. C., Murrell, J. C., Salmond, G. P. C., Dalton, H., and Lees, V. (1989) Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath), Arch. Microbiol. 152, 154-159.
25. Massey, V., and Hemmerich, P. (1980) Active-site probes of flavoproteins, Biochem. Soc. Trans. 8, 246-257.
26. Blazyk, J. L., Gassner, G. T., and Lippard, S. J., manuscript in preparation.
27. Walters, K. J., Gassner, G. T., Lippard, S. J., and Wagner, G. (1999) Structure of the soluble methane monooxygenase regulatory protein B, Proc. Natl. Acad. Sci. U.S.A. 96, 7877-7882.
28. Green, J., and Dalton, H. (1989) A stopped-flow kinetic study of soluble methane mono-oxygenase from Methylococcus capsulatus (Bath), Biochem. J. 259, 167-172.
29. Müller, J., Lugovskoy, A. A., Wagner, G., and Lippard, S. J. (2002) NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase, Biochemistry 41, 42-51.
30. Paulsen, K. E., Liu, Y., Fox, B. G., Lipscomb, J. D., Münck, E., and Stankovich, M. T. (1994) Oxidation-reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b, Biochemistry 33, 713-722.
31. Müller, F. (1992) Nuclear Magnetic Resonance Studies on Flavoproteins, in Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.) pp 557-595, CRC Press, Boca Raton, FL.
32. Ludwig, M. L., Schopfer, L. M., Metzger, A. L., Pattridge, K. A., and Massey, V. (1990) Structure and oxidation-reduction behavior of 1-deaza-FMN flavodoxins: modulation of redox potentials in flavodoxins, Biochemistry 29, 10364-10375.
33. Geoghegan, S. M., Mayhew, S. G., Yalloway, G. N., and Butler, G. (2000) Cloning, sequencing and expression of the gene for flavodoxin from Megasphaera elsdenii and the effects of removing the protein negative charge that is closest to N(1) of the bound FMN, Eur. J. Biochem. 267, 4434-4444.
34. Swenson, R. P., and Zhou, Z. (1997) Role of Electrostatic Interactions in the Regulation of the One-Electron Reduction Potentials in the Desulfovibrio Flavodoxin, in Flavins and Flavoproteins (Stevenson, K. J., Massey, V., and Williams, C. H., Jr., Eds.) pp 427-436, University of Calgary Press, Calgary, AB.
35. Bradley, L. H., and Swenson, R. P. (1999) Role of glutamate-59 hydrogen bonded to N(3)H of the flavin mononucleotide cofactor in the modulation of the redox potentials of the Clostridium beijerinckii flavodoxin. Glutamate-59 is not responsible for the pH dependency but contributes to the stabilization of the flavin semiquinone, Biochemistry 38, 12377-12386.
36. Zhou, Z., and Swenson, R. P. (1995) Electrostatic effects of surface acidic amino acid residues on the oxidation-reduction potentials of the flavodoxin from Desulfovibrio vulgaris (Hildenborough), Biochemistry 34, 3183-3192.
37. Ermler, U., Siddiqui, R. A., Cramm, R., and Friedrich, B. (1995) Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution, EMBO J. 14, 6067-6077.
38. Prasad, G. S., Kresge, N., Muhlberg, A. B., Shaw, A., Jung, Y. S., Burgess, B. K., and Stout, C. D. (1998) The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandii, Protein Sci. 7, 2541-2549.
39. Bradley, L. H., and Swenson, R. P. (2001) Role of hydrogen bonding interactions to N(3)H of the flavin mononucleotide cofactor in the modulation of the redox potentials of the Clostridium beijerinckii flavodoxin, Biochemistry 40, 8686-8695.
40. Zhou, Z., and Swenson, R. P. (1996) The cumulative electrostatic effect of aromatic stacking interactions and the negative electrostatic environment of the flavin mononucleotide binding site is a major determinant of the reduction potential for the flavodoxin from Desulfovibrio vulgaris [Hildenborough], Biochemistry 35, 15980-15988.
41. Hoover, D. M., Drennan, C. L., Metzger, A. L., Osborne, C., Weber, C. H., Pattridge, K. A., and Ludwig, M. L. (1999) Comparisons of wild-type and mutant flavodoxins from Anacystis nidulans. Structural determinants of the redox potentials, J. Mol. Biol. 294, 725-743.
42. Ludwig, M. L., Pattridge, K. A., Metzger, A. L., Dixon, M. M., Eren, M., Feng, Y., and Swenson, R. P. (1997) Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes, Biochemistry 36, 1259-1280.
43. + reductase, Nat. Struct. Biol. 8, 117-121.