Metabolic Aspects of Aerobic Obligate Methanotrophy{star, open}

Advances in Applied Microbiology

Volumn 63, Issue , 2008, Pages 183-229

  Trotsenko, Yuri A ^a   Murrell, John Colin ^b  

^a SKRYABIN INSTITUTE OF BIOCHEMISTRY AND PHYSIOLOGY OF MICROORGANISMS   (Russian Federation)

^b UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FORMALDEHYDE; FORMIC ACID; METHANE MONOOXYGENASE; METHANOL DEHYDROGENASE; PTERIN;

AEROBIC BACTERIUM; BIOCHEMISTRY; CHEMICAL ANALYSIS; CHEMICAL STRUCTURE; CRYSTAL STRUCTURE; ENZYME METABOLISM; GAMMAPROTEOBACTERIA; GENETIC ORGANIZATION; METABOLISM; METHANOTROPH; METHYLOBACTERIUM; NITROGEN FIXATION; NONHUMAN; OXIDATION; REVIEW;

AEROBIOSIS; CARBON; GRAM-NEGATIVE BACTERIA; METHANE; NITROGEN;

EID: 41349106563     PISSN: 00652164     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2164(07)00005-6     Document Type: Review

References (215)

1. Adeosun E.K., Smith T.J., Hoberg A.-M., Velarde G., Ford R., and Dalton H. Formaldehyde dehydrogenase preparations from Methylococcus capsulatus (Bath) comprise methanol dehydrogenase and methylene tetrahydromethanopterin dehydrogenase. Microbiology 150 (2004) 707-713
2. Ali M.H., Scanlan J., Dumont M.G., and Murrell J.C. Duplication of soluble methane monooxygenase genes in Methylosinus sporium and mutational analysis of the mmo operon. Microbiology 152 (2006) 2931-2942
3. i-dependent phosphofructokinase isoenzymes in the methylotrophic actinomycete Amycolatopsis methanolica. J. Bacteriol. 183 (2001) 7231-7240
4. Anthony C. The Biochemistry of Methylotrophs (1982), Academic Press, New York
5. Anthony C. Assimilation of carbon in methylotrophs. In: Goldberg I., and Rokem J.S. (Eds). "Biology of Methylotrophs" (1991), Butterworth-Heinemann, Stoneham 79-89
6. Anthony C., Ghosh M., and Blake C.C.F. The structure and function of methanol dehydrogenase and related quinoproteins containing pyrrolo-quinoline quinone. Biochem. J. 304 (1994) 665-674
7. Anthony C., and Williams P. The structure and mechanism of methanol dehydrogenase. Biochim. Biophys. Acta 1647 (2003) 18-23
8. Auman A.J., and Lidstrom M.E. Analysis of sMMO-containing type I methanotrophs in Lake Washington sediment. Environ. Microbiol. 9 (2000) 517-524
9. Auman A.J., Speake C.C., and Lidstrom M.E. nifH sequence and nitrogen fixation in type I and type II methanotrophs. Appl. Environ. Microbiol. 67 (2001) 4009-4016
10. Bastien C., Machlin S., Zahn Y., Donaldson R., and Hanson R.S. Organization of genes required for oxidation of methanol to formaldehyde in three II type methanotrophs. Appl. Environ. Microbiol. 55 (1989) 3124-3130
11. Basu P., Katterle B., Andersson K.K., and Dalton H. The membrane-associated form of methane monooxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein. Biochem. J. 369 (2003) 417-427
12. Baxter N.J., Hirt R.P., Bodrossy L., Kovacs K.L., Embley T.M., Prosser J.I., and Murrell J.C. The ribulose-1,5-bisphosphate carboxylase/oxygenase gene cluster of Methylococcus capsulatus (Bath). Arch. Microbiol. 177 (2002) 279-289
13. Bergmann D.J., Zahn J.A., and DiSpirito A.A. High-molecular-mass multi-c-heme cytochromes from Methylococcus capsulatus Bath. J. Bacteriol. 181 (1999) 991-997
14. Berven F.S., Karlsen O.A., Straume A.H., Flikka K., Murrell J.C., Fjellbirkeland A., Lillehaug I., Eidhammer I., and Jensen H.B. Analysing the outer membrane subproteome of Methylococcus capsulatus (Bath) using proteomics and novel biocomputing tools. Arch. Microbiol. 184 (2006) 362-377
15. Beschastny A.P., Sokolov A.P., Khmelenina V.N., and Trotsenko Y.A. Purification and properties of pyrophosphate-dependent phosphofructokinase of obligate methanotroph Methylomonas methanica. Biochemistry 57 (1992) 1215-1221 (Moscow)
16. Bodrossy L., Holmes E.M., Holmes A.J., Kovacs K.L., and Murrell J.C. Analysis of 16S rRNA and methane monooxygenase gene sequences reveals a novel group of thermotolerant and thermophilic methanotrophs, Methylocaldum gen. nov. Arch Microbiol. 168 (1997) 493-503
17. Bodrossy L., Kovacs K.L., McDonald I.R., and Murrell J.C. A novel thermophilic methane-oxidizing α-Proteobacterium. FEMS Microbiol. Ecol. 170 (1999) 335-341
18. Bodrossy L., Murrell J.C., Dalton H., Kalman M., Puskas L.G., and Kovacs K.L. Heat-tolerant methanotrophic bacteria from the hot-water effluent of a natural-gas field. Appl. Environ. Microbiol. 61 (1995) 3549-3555
19. Bolbot J.A., and Anthony C. The metabolism of pyruvate by the facultative methylotroph Pseudomonas AM1. J. Gen. Microbiol. 120 (1980) 233-244
20. Borodina E., Nichol T., Dumont M.G., Smith T.J., and Murrell J.C. Mutagenesis of the "leucine gate" to explore the basis of catalytic versatility in soluble methane monooxygenase. Appl. Environ. Microbiol. 73 (2007) 6460-6467
21. Bowman J.P., McCammon S.A., and Skerratt J.H. Methylosphaera hansonii gen. nov., sp. nov., a psychrophilic, group I methanotroph from Antarctic, marine salinity, meromictic lakes. Microbiology 143 (1997) 1451-1459
22. Bowman J.P., Sly L.I., Nichols P.D., and Hayward A.C. Revised taxonomy of the methanotrophs: Description of Methylobacter gen.nov., emendation of Methylococcus, validation of Methylosinus and Methylocystis species, and a proposal that the family Methylococcaceae includes only the group I methanotrophs. Int. J. Syst. Bacteriol. 43 (1993) 735-753
23. Bowman J.P., Sly L.I., and Stackebrandt E. The phylogenetic position of the family Methylococcaceae. Int. J. Syst. Bacteriol. 45 (1995) 182-185
24. Brown L.R., Strawinski R.J., and McCleskey C.S. The isolation and characterization of Methanomonas methanooxidans Brown and Strawinski. Can. J. Microbiol. 10 (1964) 791-799
25. Bulygina E.S., Kuznetsov B.B., Marusina A.I., Turova T.P., Kravchenko I.K., Bykova S.A., Kolganova T.V., and Galchenko V.F. Studies of nucleotide sequences of nifH genes in methanotrophs. Mikrobiologiya 71 (2002) 500-508
26. Cardy D.L., and Murrell J.C. Cloning, sequencing and expression of the glutamine synthetase structural gene (glnA) from the obligate methanotroph Methylococcus capsulatus (Bath). J. Gen. Microbiol. 136 (1990) 343-352
27. Cavanaugh C.M., Levering P.R., Maki J.S., and Lidstrom M.E. Symbiosis of methylotrophic bacteria and deep-sea mussels. Nature 325 (1987) 346-348
28. Chan S.I., Chen K.H.C., Yu S.S.F., Chen C.L., and Kuo S.S.J. Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria. Biochemistry 43 (2004) 4421-4430
29. Chang A.K.-C., Lim C.Y., Kim S.W., You H.J., Hahm K.S., Yoon S.M., Park J.K., and Lee J.S. Purification and characterization of two forms of methanol dehydrogenases from a marine methylotroph. J. Basic Microbiol. 42 (2002) 238-245
30. Chen Y.P., and Yoch D.C. Reconstitution of the electron transport system that couples formate oxidation to nitrogenase in Methylosinus trichosporium OB3b. J. Gen. Microbiol. 134 (1988) 3123-3128
31. + reductase from Methylosinus trichosporium OB3b. J. Bacteriol. 171 (1989) 5012-5016
32. 1-oxidizing enzymes in obligate methanotrophs. Mikrobiologiya 50 (1981) 446-452
33. Chetina E.V., and Trotsenko Y.A. Activity of oxidative phosphorylation in membranes of methanotrophic bacteria. Mikrobiologiya 55 (1986) 539-542
34. Childress J.J., Fisher C.R., Brooks J.M., Kennicutt M.C.I., Bidigare R., and Anderson A.E. A methanotrophic marine molluscan (Bivalvia, Mytilidae) symbiosis: Mussels fueled by gas. Science 233 (1986) 1306-1308
35. Chistoserdova L., Chen S.W., Lapidus A., and Lidstrom M.E. Methylotrophy in Methylobacterium extorquens AM1 from a genomic point of view. J. Bacteriol. 185 (2003) 2980-2987
36. Chistoserdova L., Lapidus A., Han C., Goodwin L., Saunder L., Brettin T., Tapa R., Gilna P., Lucas S., Richrdson P.M., and Lidstrom M.E. The genome of Methylobacillus flagellatus, the molecular basis for obligate methylotrophy, and the polyphyletic origin of methylotrophy. J. Bacteriol. 189 11 (2007) 4020-4027
37. Chistoserdova L., Laukel M., Portais J.C., Vorholt J.A., and Lidstrom M.E. Multiple formate dehydrogenase enzymes in the facultative methylotroph Methylobacterium extorquens AM1 are dispensable for growth on methanol. J. Bacteriol. 186 (2004) 22-28
38. Chistoserdova L., Vorholt J.A., Thauer R.K., and Lidstrom M.E. C1 transfer enzymes and coenzymes linking methylotrophic bacteria and methanogenic archae. Science 281 (1998) 99-102
39. Choi D.W., Antholine W.E., Do Y.S., Semrau J.D., Kisting C.J., Kunz R.C., Campbell D., Rao V., Hartsel S.C., and DiSpirito A.A. Effect of methanobactin on the activity and electron paramagnetic resonance spectra of the membrane-associated methane monooxygenase in Methylococcus capsulatus Bath. Microbiology 151 (2005) 3417-3426
40. Choi D.W., Do Y.S., Zea J.C., McEllistream M.T., Lee S.W., Semrau J.D., Pohl N.L., Kisting C.J., Scardino L.L., Hartsel S.C., Boyd E.S., Geesey G.G., et al. Spectral and thermodynamic properties of Ag(I), Au(III), Cd(II), Co(II), Fe(III), Hg(II), Mn(II), Ni(II), Pb(II), U(IV), and Zn(II) binding by methanobactin from Methylosinus trichosporium OB3b. J. Inorg. Biochem. 100 (2006) 2150-2161
41. Colby J., and Dalton H. Some properties of soluble methane monooxygenase from Methylococcus capsulatus (Bath). Biochem. J. 171 (1976) 461-468
42. Colby J., Stirling D.I., and Dalton H. The soluble methane monooxygenase of Methylococcus capsulatus (Bath). Biochem. J. 165 (1977) 395-402
43. Crabarse W., Mahlert F., Shima S., Thauer R.K., and Ermler U. Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: Unusual amino acid modification, conservation and adaptation. J. Mol. Biol. 303 (2000) 329-344
44. Csaki R., Bodrossy L., Klem J., Murrell J.C., and Kovacs K.L. Genes involved in the copper-dependent regulation of soluble methane monooxygenase of Methylococcus capsulatus (Bath): Cloning, sequencing and mutational analysis. Microbiology 149 (2003) 1785-1795
45. Dalton H. The Leeuwenhoek Lecture (2000). The natural and unnatural history of methane oxidizing bacteria. Phil. Trans. R. Soc. B. 360 (2005) 1207-1222
46. Davey J.F., Whittenbury R., and Wilkinson J.F. The distribution in the methylobacteria of some key enzymes concerned with intermediary metabolism. Arch. Microbiol. 87 (1972) 359-366
47. Dedysh S.N., Khmelenina V.N., Suzina N.E., Trotsenko Y.A., Semrau J.D., Liesack W., and Tiedje J.M. Methylocapsa acidiphila gen nov. sp. nov., a novel methane-oxidizing and dinitrogen-fixing acidophilic bacterium from Sphagnum bog. Int. J. Syst. Evol. Microbiol. 52 (2002) 251-261
48. Dedysh S.N., Liesack W., Khmelenina V.N., Suzina N.E., Trotsenko Y.A., Semrau J.D., Bares A.M., Panikov N.S., and Tiedje J.M. Methylocella palustris gen. nov., sp. nov., a new methane-oxidizing acidophilic bacterium from peat bogs, representing a novel subtype of serine-pathway methanotrophs. Int. J. Syst. Evol. Microbiol. 50 (2000) 955-969
49. Dedysh S.N., Knief C., and Dunfield P. Methylocella species are facultatively methanotrophic. J. Bacteriol. 187 (2005) 4665-4667
50. Dedysh S.N., Ricke P., and Liesack W. NifH and NifD phylogenies: An evolutionary basis for understanding nitrogen fixation capabilities of methanotrophic bacteria. Microbiology 150 (2004) 1301-1313
51. Dijkhuizen L., Harder W., and de Boyer L. Genetic manipulation of restricted facultative methylotroph Hyphomicrobium by the R-plasmid mediated introduction. Arch. Microbiol. 139 (1984) 311-318
52. DiSpirito A.A., Zahn J.A., Graham D.W., Kim H.J., Larive C.K., Derrick T.S., Cox C.D., and Taylor A. Copper-binding compounds from Methylosinus trichosporium OB3b. J. Bacteriol. 180 (1998) 3606-3613
53. Dumont C.G., and Murrell J.C. Stable isotope probing - linking microbial identity to function. Nat. Rev. Microbiol. 3 (2005) 499-504
54. Dunfield P.F., Khmelenina V.N., Suzina N.E., Trotsenko Y.A., and Dedysh S.N. Methylocella silvestris sp. nov., a novel methanotroph isolated from an acidic forest cambisol. Int.J. Syst. Evol. Microbiol. 53 (2003) 1231-1239
55. Dunfield P.F., Tchawa Yimga M., Dedysh S.N., Berger U., Liesack W., and Heyer J. Isolation of a Methylocystis strain containing a novel pmoA-like gene. FEMS Microbiol. Ecol. 41 (2002) 17-26
56. Dunfield P.F., Yuryev A., Senin P., Smirnova A.V., Stott M.B., Hou S., Ly B., Saw J.H., Zhou Z., Ren Y., Wang J., Mountain B.W., et al. Methane oxidation by an extremely acidophilic bacterium of the phylum Verrucomicrobia. Nature 450 (2007) 879-882
57. Dworkin M., and Foster J.W. Studies on Pseudomonas methanica (Söhngen) nov.comb. J. Bacteriol. 72 (1956) 646-659
58. Eccleston M., and Kelly D.P. Assimilation and toxicity of exogenous amino acids in the methane-oxidizing bacterium Methylococcus capsulatus. J. Gen. Microbiol. 71 (1972) 541-544
59. 1-compounds, alcohols, sugars and acetate in the methane-oxidizing bacterium Methylococcus capsulatus. J. Gen. Microbiol. 75 (1973) 211-221
60. Eccleston M., and Kelly D.P. Inhibition by l-threonine of aspartokinase as a cause of threonine toxicity to Methylococcus capsulatus. J. Gen. Microbiol. 75 (1973) 223-226
61. Erb T.J., Berg I.A., Brecht V., Müller M., Fuchs G., and Alber B.E. Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase reductase: the ethylmalonyl-CoA pathway. Proc. Natl. Acad. Sci. USA 104 (2007) 10631-10636
62. Eshinimaev B.Ts., Medvedkova K.A., Khmelenina V.N., Suzina N.E., Osipov G.A., Lysenko A.M., and Trotsenko Y.A. New thermophilic methanotrophs of the Methylocaldum genus. Mikrobiologiya 73 (2004) 448-456
63. Ferenci T., Strom T., and Quayle J.R. Purification and properties of 3-hexulose phosphate synthase from Methylococcus capsulatus. Biochem. J. 144 (1974) 477-486
64. Foster J.W., and Davis R.H. A methane-dependent coccus, with notes on classification and nomenclature of obligate methane-utilizing bacteria. J. Bacteriol. 91 (1966) 1924-1931
65. Fox B.G., Bornemann J.G., Wackett L.P., and Lipscomb J.D. Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: Mechanistic and environmental applications. Biochemistry 29 (1990) 6419-6437
66. Fox B.G., Froland J.E., Dege J., and Lipscomb J.D. Methane monooxygenase from Methylosinus trichosporium OB3b: Purification and properties of a three component system with high specific activity from a type II methanotroph. J. Biol. Chem. 264 (1989) 10023-10033
67. Fuse H., Ohta M., Takimura O., Murakami K., Inoue H., Yamaoka Y., Oclarit J.M., and Omori T. Oxidation of trichloroethylene and dimethyl sulfide by a marine Methylomicrobium strain containing soluble methane monooxygenase. Biosci. Biotechnol. Biochem. 62 (1998) 1925-1931
68. Gilbert B., McDonald I.R., Stafford G.P., Finch R., Nielsen A.K., and Murrell J.C. Molecular analysis of the pmo (particulate methane monooxygenase) operons from two type II methanotrophs. Appl. Environ. Microbiol. 66 (2000) 966-975
69. Goodwin P.M., and Anthony C. The biosynthesis of periplasmic electron transport protein in methylotrophic bacteria. Microbiology 141 (1995) 1051-1064
70. Green J., and Dalton H. Protein B of soluble methane monooxygenase from Methylococcus capsulatus Bath. J. Biol. Chem. 260 (1985) 15795-15801
71. Grosse S., Laramee L., Wendlandt K.-D., McDonald I.R., Miguez C.B., and Kleber H.-P. Purification and characterization of the soluble methane monooxygenase of the type II methanotrophic bacterium Methylocystis sp. strain Wl 14. Appl. Environ. Microbiol. 65 (1999) 3929-3935
72. Hagemeier C.H., Chistoserdova L., Lidstrom M.E., Thauer R.K., and Vorholt J.A. Characterization of the second methylene tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1. Eur. J. Biochem. 267 (2000) 3762-3769
73. Hakemian A.S., and Rosenzweig A.C. The biochemistry of methane oxidation. Annu Rev. Biochem. 76 (2007) 223-241
74. Hanson R.S., and Hanson T.E. Methanotrophic bacteria. Microbiol. Rev. 60 (1996) 439-471
75. Heyer J., Berger U., Hardt M., and Dunfield P. Methylohalobius crimeensis gen. nov., sp. nov., a moderately halophilic, methanotrophic bacterium isolated from hypersaline lakes of Crimea. Int. J. Syst. Evol. Microbiol. 55 (2005) 1817-1826
76. Heyer J., Galchenko V.F., and Dunfield P.F. Molecular phylogeny of type II methane oxidizing bacteria isolated from various environments. Microbiology 148 (2002) 2831-2846
77. Higgins I.J., Best D.J., and Hammond R.C. New findings in methane-utilizing bacteria highlight their importance in the biosphere and their commercial potential. Nature 286 (1980) 561-564 (London)
78. Higgins I.J., Best D.J., Hammond R.C., and Scott D. Methane-oxidizing microorganisms. Microbiol. Rev. 43 (1981) 556-590
79. Higgins I.J., and Quayle J.R. Oxygenation of methane by methane-grown Pseudomonas methanica and Methanomonas methanooxidans. Biochem. J. 118 (1970) 201-208
80. Holmes A.J., Lidstrom M.E., and Murrell J.C. Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionary related. FEMS Microbiol. Lett. 132 (1995) 203-208
81. Islam T., Jensen S., Reigstad L.J., Larsen O., and Birkeland N.-K. Methane oxidation at 55 °C and pH 2 by a thermoacidophilic bacterium belonging to the Verrucomicrobia phylum. Proc. Natl. Acad. Sci. (USA) 105 (2008) 3000-3004
82. Kalyuzhnaya M.G., Khmelenina V.N., Eshinimaev B.C., Suzina N.E., Nikitin D., Solonin A., Lin J.L., McDonald I.R., Murrell J.C., and Trotsenko Y.A. Taxonomic characterization of new alkaliphilic and alkalitolerant methanotrophs from soda lakes of the Southeastern Transbaikal region and description of Methylomicrobium buryatense sp. nov. Syst. Appl. Microbiol. 24 (2001) 166-176
83. Kao W.-C., Chen Y.-R., Yi E.C., Lee H., Tian Q., Wu K.-M., Tsai S.-F., Yu S.S.-F., Chen Y.J., Aebersold R., and Chan S.I. Quantitative proteomic analysis of metabolic regulation by copper ions in Methylococcus capsulatus (Bath). J. Biol. Chem. 279 (2005) 51554-51560
84. Kaserer H. Uber die Oxidation des Wasserstoffes und des Methan durch Mikroorganismen. (The oxidation of hydrogen and methane by microorganisms). Z. landw. Versuchsw. in Osterreich. 8 (1905) 789-792
85. Kaserer H. Uber die Oxidation des Wasserstoffes und des Methane durch Mikroorganismes. (The oxidation of hydrogen and methane by microorganisms). Zbl. Bakt. Parasitenk. 15 (1906) 573-576
86. Kato N., Yurimoto H., and Thauer R.K. The physiological role of the ribulose monophosphate pathway in bacteria and Archaea. Biosci. Biotech. Biochem. 70 (2006) 10-21
87. Kelly D.P., Anthony C., and Murrell J.C. Insights into the obligate methanotroph Methylococcus capsulatus. Trends Microbiol. 13 (2005) 195-198
88. Khmelenina V.N., Kalyuzhnaya M.G., Starostina N.G., Suzina N.E., and Trotsenko Y.A. Isolation and characterization of halotolerant alkaliphilic methanotrophic bacteria from Tuva soda lakes. Curr. Microbiol. 35 (1997) 257-261
89. Khmelenina V.N., Kalyuzhnaya M., Suzina N.E., Trotsenko Y.A., and Gottschalk G. Osmoadaptation in halophilic and alkaliphilic methanotrophs. Arch. Microbiol. 172 (1999) 321-329
90. Kim H.J., Galeva N., Larive C.K., Alterman M., and Graham D.W. Purification and physical-chemical properties of methanobactin: A chalkophore from Methylosinus trichosporium OB3b. Biochemistry 44 (2005) 5140-5148
91. Kim H.J., Graham D.W., DiSpirito A.A., Alterman M.A., Galeva N., Larive C.K., and Asunskis D. Methanobactin, a copper-acquisition compound from methane-oxidizing bacteria. Science 305 (2004) 1612-1615
92. Kitmitto A., Myronova N., Basu P., and Dalton H. Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath). Biochemistry 44 (2005) 10954-10965
93. Kletsova L.V., Govorukhina N.I., Tsygankov Y.D., and Trotsenko Y.A. Metabolism of obligate methylotroph Methylobacillus flagellatum. Mikrobiologiya 56 (1987) 901-906
94. Klotz M.G., and Norton J.M. Multiple copies of ammonia monooxygenase (amo) operons have evolved under biased AT/GC mutational pressure. FEMS Microbiol. Lett. 132 (1998) 303-311
95. Korotkova N., and Lidstrom M.E. Glyoxylate regeneration pathway in the methylotroph Methylobacterium extorquens AM1. J. Bacteriol. 184 (2002) 1750-1758
96. Large P.J., and Bamforth C.W. Methylotrophy and biotechnology (1988), Longman Higher Education, Harlow (UK) 324
97. Lawrence A.J., Kemp M.B., and Quayle J.R. Synthesis of cells constituents by methane-grown Methylococcus capsulatus and Methylomonas methanooxidans. Biochem. J. 116 (1970) 631-639
98. Lawrence A.J., and Quayle J.R. Alternative carbon assimilation pathways in methane-utilizing bacteria. J. Gen. Microbiol. 63 (1970) 371-374
99. Leak D.J., Stanley S.H., and Dalton H. Implication of the nature of methane monooxygenase on carbon assimilation in methanotrophs. In: Poole R.K., and Dow C.S. (Eds). "Microbial Gas Metabolism, Mechanistic, Metabolic and Biotechnological aspects" (1985), Academic Press, London 201-208
100. Lidstrom M.E. Isolation and characterization of marine methanotrophs. Anton. Leeuwenhoek 54 (1988) 189-199
101. Lidstrom M.E. Genetics of carbon metabolism in methylotrophic bacteria. FEMS Microbiol. Rev. 87 (1990) 431-436
102. Lieberman R.L., and Rosenzweig A.C. Biological methane oxidation: Regulation, biochemistry and active site structure of particulate methane monooxygenase. Crit. Rev. Biochem. Mol. Biol. 39 (2004) 147-164
103. Lieberman R.L., and Rosenzweig A.C. Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 434 (2005) 177-182
104. Lieberman R.L., Shrestha D.B., Doan P.E., Hoffman B.M., Stemmler T.L., and Rosenzweig A.C. Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and copper-containing clusters. Proc. Natl. Acad. Sci. USA. 100 (2003) 3820-3825
105. Malashenko Y.R. Isolation and characterization of new species (thermophilic and thermotolerant ones) of methane utilizers. In: Schlegel H.G., Gottschalk G., and Pfenning N. (Eds). "Microbial Production and Utilisation of Gases" (1976), E. Goltze KG, Gottingen 293-300
106. Malashenko Y.R., Pinchuk G.E., and Sokolov I.G. The activity of Methylococcus thermophilus aspartate kinase regulated by amino acids of the aspartate family. Mikrobiologiya 56 (1987) 740-745
107. McDonald I.R., Kenna E.M., and Murrell J.C. Detection of methanotrophic bacteria in environmental samples with the PCR. Appl. Environ. Microbiol. 61 (1995) 116-121
108. McDonald I.R., Miguez C.B., Rogge G., Bourque D., Wendlandt K.D., Groleau D., and Murrell J.C. Diversity of soluble methane monooxygenase-containing methanotrophs isolated from polluted environments. FEMS Microbiol. Lett. 255 (2006) 225-232
109. McDonald I.R., and Murrell C.J. The methanol dehydrogenase structural gene mxaF and its use as a functional gene probe for methanotrophs and methylotrophs. Appl. Environ. Microbiol. 63 (1997) 3218-3224
110. Meister M., Saum S., Alber B.E., and Fuchs G. l-Malyl-Coenzyme A/β-methylmalyl-coenzyme A lyase is involved in acetate assimilation of the isocitrate lyase-negative bacterium Rhodobacter capsulatus. J. Bacteriol. 187 (2005) 1415-1425
111. Mitsui R., Sakai Y., Yasueda H., and Kato N. A novel operon encoding formaldehyde fixation: The ribulose monophosphate pathway in the gram-positive facultative methylotrophic bacterium Mycobacterium gastrii MB19. J. Bacteriol. 182 (2000) 944-948
112. Murrell J.C., and Dalton H. Nitrogen fixation in obligate methanotrophs. J. Gen. Microbiol. 129 (1983) 3481-3486
113. Murrell J.C., and Dalton H. Ammonia assimilation in Methylococcus capsulatus (Bath) and other obligate methanotrophs. J. Gen. Microbiol. 129 (1983) 1197-1206
114. Murrell J.C., and Dalton H. Purification and properties of glutamine synthetase from Methylococcus capsulatus (Bath). J. Gen. Microbiol. 129 (1983) 1187-1196
115. Murrell J.C., and Dalton H. Methane and methanol utilizers. In: Atkinson T., and Sherwood R.F. (Eds). "Biotechnology Handbooks" (1992), Plenum Press, London 286
116. Murrell J.C., Gilbert B.B., and McDonald I.R. Molecular biology and regulation of methane monooxygenase. Arch. Microbiol. 173 (2000) 325-332
117. Murrell J.C., McDonald I.R., and Bourne D.G. Molecular methods for the study of methanotroph ecology. FEMS Microbiol. Ecol. 27 (1998) 103-114
118. Murrell J.C., McDonald I.R., and Gilbert B. Regulation of expression of methane monooxygenases by copper ions. Trends Microbiol. 8 (2000) 221-225
119. Myronova N., Kitmitto A., Collins R.F., Miyaji A., and Dalton H. Three-dimensional structure determination of a protein supercomplex that oxidizes methane to formaldehyde in Methylococcus capsulatus (Bath). Biochemistry 45 (2006) 11905-11914
120. Nguyen H.H., Shiemke A.K., Jacobs S.J., Hales B.J., Lidstrom M.E., and Chan S.I. The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 269 (1994) 14995-15005
121. Nguyen H.T., Elliott S.J., Yip J.H., and Chan S.I. The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. J. Biol. Chem. 273 (1998) 7957-7978
122. Nielsen A.K., Gerdes K., Degn H., and Murrell J.C. Regulation of bacterial oxidation: Transcription of the soluble operon of Methylococcus capsulatus (Bath) is repressed by copper ions. Microbiology 142 (1996) 1289-1296
123. Oakley C.J., and Murrell J.C. nifH genes in the obligate methane oxidizing bacteria. FEMS Microbiol. Lett. 49 (1988) 53-57
124. Oakley C.J., and Murrell J.C. Cloning of nitrogenase structural genes from obligate methanotroph Methylococcus capsulatus (Bath). FEMS Microbiol. Lett. 62 (1991) 121-125
125. Omelchenko M.B., Vasilieva L.V., Zavarzin G.A., Savelieva N.D., Lysenko A.M., Mityushina L.L., Khmelenina V.N., and Trotsenko Y.A. A novel psychrophilic methanotroph of the genus Methylobacter. Mikrobiologiya 65 (1996) 339-343
126. Omelchenko M.V., Vasilieva L.V., and Zavarzin G.A. Psychrophilic methanotroph from tundra soil. Curr. Microbiol. 27 (1993) 255-259
127. Patel R.N., and Felix A. Microbial oxidation of methane and methanol: Crystallization and properties of methanol dehydrogenase from Methylosinus sporium. J. Bacteriol. 128 (1978) 413-424
128. Patel R., Hoare S.L., Hoare D.S., and Taylor B.F. Incomplete tricarboxylic acid cycle in a type I methylotroph Methylococcus capsulatus. J. Bacteriol. 123 (1975) 382-384
129. 14C] Acetate assimilation by a type I obligate methylotroph, Methylococcus capsulatus. Appl. Environ. Microbiol. 34 (1977) 607-610
130. Patel R.N., Hou C., and Felix A. Microbial oxidation of methane and methanol: Crystallization of methanol dehydrogenase and properties of holo- and apo-methanol dehydrogenase from Methylomonas methanica. J. Bacteriol. 133 (1978) 641-649
131. Pinchuk G.E., Schurova Z.P., Shatokhina E.S., Mozhilevskaya L.P., Sokolov I.G., and Malashenko Y.R. Growth of the methane-oxidizing bacterium Methylococcus thermophilus in the presence of aminoacids belonging to the aspartate family. Mikrobiologiya 56 (1987) 621-625
132. Pol A., Heijmans K., Harhangi H.R., Tedesco D., Jetten M.S., and Op den Camp H.J. Methanotrophy below pH 1 by a new Verrucomicrobia species. Nature 450 (2007) 874-878
133. Pomper B.K., and Vorholt J.A. Characterization of the formyltransferase (Ftr) from Methylobacterium extorquens AM1. Eur. J. Biochem. 269 (2001) 769-4775
134. +-dependent formate dehydrogenase. Biochem. J. 301 (1994) 625-643
135. 1 compounds. Proc. Biochem. 2 (1969) 25-29
136. Quayle J.R. The metabolism of the one-carbon compounds by microorganisms. Adv. Microbial Physiol. 7 (1972) 119-203
137. Quayle J.R. The microbial assimilation of C1 compounds. Biochem. Soc. Trans. 8 (1980) 1-10
138. Quayle J.R., and Ferenci T. Evolutionary aspects of autotrophy. Microbiol. Rev. 42 (1978) 251-273
139. Raghoebarsing A.A., Smolders A.J.P., Schmid M.C., Rijpstra W.R.C., Wolters-Arts M., Derksen J., Jetten M.S.M., Schouten S., Damste J.S.S., Lamers L.P.M., Roelofs J.G.M., Op den Camp H.J.M., et al. Methanotrophic symbionts provide carbon for photosynthesis in peat bogs. Nature 436 (2005) 1153-1156
140. 1 Compounds" (1993), Intercept Press, Andover, UK 1-14
141. Reshetnikov A.S., Mustakhimov I.I., Khmelenina V.N., Beschastny A.P., and Trotsenko Y.A. Identification and cloning of the gene of pyrophosphate dependent 6-phosphofructokinase from Methylomonas methanica. Doklady Biochem. Biophys. 405 (2005) 468-470
142. Ricke P., Erkel C., Kube M., Reinhardt R., and Liesack W. Comparative analysis of the conventional and novel pmo (particulate methane monooxygenase) operons from Methylocystis strain SC2. Appl. Environ. Microbiol. 70 (2004) 3055-3063
143. Sakai Y., Mitsui R., Katayama Y., Yanase H., and Kato N. Organization of the genes involved in the ribulose monophosphate pathway in an obligate methylotrophic bacterium, Methylomonas aminofaciens 77a. FEMS Microbiol. Lett. 176 (1999) 125-130
144. Semrau J.D., Chistoserdov A., Lebron J., Costello A., Davagnino J., Kenna E., Holmes A.J., Finch R., Murrell J.C., and Lidstrom M.E. Particulate methane monooxygenase genes in methanotrophs. J. Bacteriol. 177 (1995) 3071-3079
145. Sharpe P.L., Koffas M., Wilczek J., Knoke K., and Odom J.M. Genomic and genetic analysis of central carbon metabolism in the obligate methanotroph Methylomonas sp. 16A. Abstract of papers presented at the meeting on Molecular Genetics of Bacteria and Phages., Washington, DC (2002) 115
146. Shiemke A.K., Cook S.A., Miley T., and Singleton P. Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors. Arch. Biochem. Biophys. 321 (1995) 421-428
147. Shishkina V.N., and Trotsenko Y.A. Pathways of ammonia assimilation in obligate methane utilizers. FEMS Microbiol. Lett. 5 (1979) 187-191
148. Shishkina V.N., and Trotsenko Y.A. Multiple enzymic lesions in obligate methanotrophic bacteria. FEMS Microbiol. Lett. 13 (1982) 237-242
149. Shishkina V.N., and Trotsenko Y.A. The levels of carbon dioxide assimilation by methanotrophic bacteria. Mikrobiologiya 55 (1986) 377-382
150. Shishkina V.N., Yurchenko V.V., Romanovskaya V.A., Malashenko Y.R., and Trotsenko Y.A. Alternativity of methane assimilation pathways in obligate methylotrophs. Mikrobiologiya 45 (1976) 417-419
151. Smith D.D.S., and Dalton H. Solubilization of methane monooxygenase from Methylococcus capsulatus (Bath). Eur. J. Biochem. 182 (1989) 667-671
152. Smith T.J., and Dalton H. Biocatalysis by methane monooxygenase and its implications for the petroleum industry. Petroleum Biotechnology: Developments and Perspectives Studies in Surface Science and Catalysis 151 (2004) 177-192
153. Smith A.J., and Hoare D.S. Specialist phototrophs, lithotrophs and methylotrophs: A unity among a diversity of Procaryotes. Bacteriol. Rev. 41 (1977) 419-448
154. Smith T.J., Slade S.E., Burton N.P., Murrell J.C., and Dalton H. An improved system for protein engineering of the hydroxylase component of soluble methane monooxygenase. Appl. Environ. Microbiol. 68 (2002) 5265-5273
155. Söhngen N.L. Uber bakterien welche methan ab kohlenstoffnahrung und energiequelle gerbrauchen (On bacteria which use methane as a carbon and energy source). Z. Bakteriol. Parazitenk. (Infektionster) 15 (1906) 513-517
156. Söhngen N.L. Sur de role du methane dans la vie organique (The role of methane in organic life). Rec. trav. Chim. 29 (1910) 238-374
157. Sokolov I.G., Malashenko Y.R., and Romanovskaya V.A. Electron transport chain in thermophilic methanotroph Methylococcus thermophilus. Mikrobiologiya 50 (1981) 13-29
158. Sokolov I.G., and Romanovskaya V.A. Mechanisms of obligate methylotrophy. Mikrobiol. J. 54 (1992) 87-104
159. Sokolov A.P., and Trotsenko Y.A. Purification and characterization of 3-hexulosephosphate synthase from facultative methylotroph Pseudomonas oleovorans. Biochemistry 43 (1979) 782-787 (Moscow)
160. Sorokin D.Y., Jones B.E., and Kuenen G.J. An obligately methylotrophic, methane-oxidizing Methylomicrobium species from highly alkaline environment. Extremophiles 4 (2000) 145-155
161. Stafford G.P., Scanlan J., McDonald I.R., and Murrell J.C. Characterization of rpoN, mmoR and mmoG, genes involved in regulating the expression of soluble methane monooxygenase in Methylosinus trichosporium OB3b. Microbiology 149 (2003) 1771-1784
162. Stainthorpe A.C., Lees V., Salmond G.P.C., Dalton H., and Murrell J.C. The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath). Gene 91 (1990) 27-34
163. Stainthorpe A.C., Murrell J.C., Salmond G.P., Dalton H., and Lees V. Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath). Arch. Microbiol. 152 (1989) 154-159
164. Stainthorpe A.C., Salmond G.P., Dalton H., and Murrell J.C. Screening of obligate methanotrophs for soluble methane monooxygenase genes. FEMS Microbiol. Lett. 70 (1990) 211-216
165. Stanley S.H., and Dalton H. Role of ribulose-1,5-bisphosphate carboxylase/oxygenase in Methylococcus capsulatus (Bath). J. Gen. Microbiol. 128 (1982) 2927-2935
166. Stanley S.H., Prior S.D., Leak D.J., and Dalton H. Copper stress underlies the fundamental change in intracellular location of methane monooxygenase in methane-oxidizing organisms: Studies in batch and continuous cultures. Biotechnol. Lett. 5 (1983) 487-492
167. Stirling D., Colby J., and Dalton H. A comparison of the substrate and electron-donor specificities of the methane-monooxygenase from three strains of methane-oxidizing bacteria. Biochem. J. 177 (1979) 361-364
168. +-linked formaldehyde dehydrogenase from Methylococcus capsulatus (Bath). J. Gen. Microbiol. 107 (1978) 19-29
169. Stirling D., and Dalton H. Properties of the methane monooxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath). Eur. J. Biochem. 96 (1979) 205-212
170. Stoecker K., Bendinger B., Schoning B., Nielsen P.H., Nielsen J.L., Baranyi C., Toenshoff E.R., Daims H., and Wagner M. Cohn's Crenothrix is a filamentous methane oxidizer with an unusual methane monooxygenase. Proc. Natl. Acad. Sci. USA. 103 (2006) 2363-2367
171. Stolyar S., Costello A.M., Peeples T.L., and Lidstrom M.E. Role of multiple gene copies in particulate methane monooxygenase activity in the methane-oxidising bacterium Methylococcus capsulatus (Bath). Microbiology 145 (1999) 1235-1244
172. Stolyar S., Franke M., and Lidstrom M.E. Expression of individual copies of Methylococcus capsulatus Bath particulate methane monooxygenase genes. J. Bacteriol. 183 (2001) 1810-1812
173. Strom T., Ferenci T., and Quayle J.R. The carbon assimilation pathway of Methylococcus capsulatus, Pseudomonas methanica and Methylosinus trichosporium (OB3b). Biochem. J. 144 (1974) 465-476
174. Suzina N.E., Chetina E.V., Trotsenko Y.A., and Fikhte B.A. Peculiarities of the supramolecular organization of intracytoplasmic membranes in methanotrophs. FEMS Microbiol. Lett. 30 (1985) 111-114
175. Tate S., and Dalton H. A low-molecular-mass protein from Methylococcus capsulatus (Bath) is responsible for the regulation of formaldehyde dehydrogenase activity in vitro. Microbiology 145 (1999) 159-167
176. Taylor S.C. Evidence for the presence of ribulose-1,5-bisphosphate carboxylase and phosphoribulokinase in Methylococcus capsulatus (Bath). FEMS Microbiol. Lett. 2 (1977) 305-307
177. Taylor I.J., and Anthony C. A biochemical basis for obligate methylotrophy: Properties of a mutant of Pseudomonas AM1 lacking 2-oxoglutarate dehydrogenase. J. Gen. Microbiol. 93 (1976) 259-265
178. Taylor S.C., Dalton H., and Dow C.S. Purification and initial characterization of ribulose 1,5-bisphosphate carboxylase from Methylococcus capsulatus (Bath). FEMS Microbiol. Lett. 8 (1980) 157-160
179. Taylor S.C., Dalton H., and Dow C.S. Ribulose-1,5-bisphosphate carboxylase/oxygenase and carbon assimilation in Methylococcus capsulatus (Bath). J. Gen. Microbiol. 122 (1981) 89-94
180. Theisen A.R., Ali H.M., Radajewski S., Dumont M.G., Dunfield P.F., McDonald I.R., Dedysh S.N., Miguez C.B., and Murrell J.C. Regulation of methane oxidation in the facultative methanotroph Methylocella silvestris BL2. Mol. Microbiol. 58 (2005) 682-692
181. Theisen A.R., and Murrell J.C. Facultative methanotrophs revisited. J. Bacteriol. 187 (2005) 4303-4305
182. Tchawa Yimga M., Dunfield P.F., Ricke P., Heyer J., and Liesack W. Wide distribution of a novel pmoA-like gene copy among type II methanotrophs, and its expression in Methylocystis strain SC2. Appl. Environ. Microbiol. 69 (2003) 5593-5602
183. Tonge G.M., Harrison D.E.F., and Higgins I.J. Purification and properties of the methane monooxygenase enzyme from Methylosinus trichosporium OB3b. Biochem. J. 161 (1977) 333-344
184. Tonge G.M., Knowles C.J., Harrison D.E.F., and Higgins I.J. Metabolism of one carbon compounds. Cytochromes of methane- and methanol-utilizing bacteria. FEBS Lett. 44 (1975) 106-110
185. Toukdarian A.E., and Lidstrom M.E. Nitrogen metabolism in a new obligate methanotroph "Methylosinus" strain 6. J. Gen. Microbiol. 130 (1984) 1827-1837
186. Trotsenko Y.A. Isolation and characterization of obligate methanotrophic bacteria. In: Schlegel H.G., Gottschalk G., and Pfennig N. (Eds). "Microbial Production and Utilization of Gases" (1976), Goltze K.G., Gottingen 329-336
187. Trotsenko Y.A. Metabolic features of methane- and methanol-utilizing bacteria. Acta Biotechnol. 3 (1983) 269-277
188. Trotsenko Y.A., and Chetina E.V. Energy metabolism of methanotrophic bacteria. Adv. Microbiol. 22 (1988) 3-34
189. Trotsenko Y.A., Doronina N.V., and Khmelenina V.N. Biotechnological potential of aerobic methylotrophic bacteria: A review of current state and future prospects. Appl. Biochem. Microbiol. 41 (2005) 433-441
190. Trotsenko Y.A., Ivanova E.G., and Doronina N.V. Aerobic methylotrophic bacteria as phytosymbionts. Mikrobiologiya 70 (2001) 623-632
191. Trotsenko Y.A., and Khmelenina V.N. Biology of extremophilic and extremotolerant methanotrophs. Arch. Microbiol. 177 (2002) 123-131
192. Trotsenko Y.A., and Khmelenina V.N. Aerobic methanotrophic bacteria of cold ecosystems. FEMS Microbiol. Ecol. 53 (2005) 15-26
193. 1 Compounds" (1996), Kluwer Academic Publishers, Dordrecht 4-8
194. Trotsenko Y.A., and Shishkina V.A. Studies on phosphate metabolism in obligate methylotrophs. FEMS Microbiol. Rev. 87 (1990) 267-271
195. Tsubota J., Eshinimaev B.Ts., Khmelenina V.N., and Trotsenko Y.A. Methylothermus thermalis gen. nov., sp. nov. - a novel moderately thermophilic obligate methanotroph from a hot spring in Japan. Int. J. Syst. Evol. Microbiol. 55 (2005) 1877-1884
196. Van Spanning R.J.M., de Vries S., and Harms N. Coping with formaldehyde during C1 metabolism of Paracoccus denitrificans. J. Mol. Catalysis B: Enzymatic. 8 (2000) 37-50
197. Vigliotta G., Nutricati E., Carata E., Tredici S.M., DE Stefano M., Pontieri P., Massardo D.R., Prati M.V., DE Bellis L., and Alifano P. Clonothrix fusca (Roze, 1896). a filamentous, sheathed, methanotrophic γ-Proteobacterium. Appl Environ Microbiol. 73 11 (2007) 3356-3565
198. Vorholt J.A. Cofactor-dependent formaldehyde oxidation in methylotrophic bacteria. Arch. Microbiol. 178 (2002) 239-249
199. +-dependent methylene tetrahydromethanopterin dehydrogenase in Methylobacterium extorquens AM1. J. Bacteriol. 180 (1998) 5351-5356
200. Vorholt J.A., Chistoserdova L., Stolyar S.M., Lidstrom M.E., and Thauer R.K. Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolase. J. Bacteriol. 181 (1999) 5750-5757
201. Vorholt J.A., Kalyuzhnaya M.G., Hagemeier C.H., Lidstrom M.E., and Chistoserdova L. MtdC, a novel class of methylene tetrahydromethanopterin dehydrogenases. J. Bacteriol. 187 (2005) 6069-6074
202. Vorholt J.A., Marx C.J., Lidstrom M.E., and Thauer R.K. Novel formaldehyde activating enzyme in Methylobacterium extorquens AM1 required for growth on methanol. J. Bacteriol. 182 (2000) 6645-6650
203. Wadzinski A.M., and Ribbons D.W. Utilization of acetate by Methanomonas methanooxidans. J. Bacteriol. 123 (1975) 380-381
204. Ward N., Larsen Ø., S., J., Bruseth L., Khouri H., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M., Nelson K.E., et al. Genomic insights into methanotrophy: The complete genome sequence of Methylococcus capsulatus (Bath). PLoS Biology 2 (2004) 1616-1628
205. Whittenbury R. Microbial utilization of methane. Proc. Biochem. 4 (1969) 51-56
206. 1 Compounds" (1980), Heiden, London 181-190
207. Whittenbury R., and Kelly D.P. Autotrophy: A conceptual phoenix. Symp. Soc. Gen. Microbiol. 27 (1977) 121-149
208. Whittenbury R., Phillips K.C., and Wilkinson J.F. Enrichment, isolation and some properties of methane-utilizing bacteria. J. Gen. Microbiol. 61 (1970) 205-218
209. Wood A.P., Aurikko J.P., and Kelly D.P. A challenge for 21st century molecular biology and biochemistry: What are the causes of obligate autotrophy and methanotrophy. FEMS Microbiol. Rev. 28 (2004) 335-352
210. Woodland M.P., and Cammack R. Electron spin resonance properties of component A of the soluble methane monooxygenase from Methylococcus capsulatus (Bath). In: Poole R.K., and Dow C.S. (Eds). "Microbial Gas Metabolism" (1985), Academic Press, London 182-213
211. Xing X.-H., Wu H., Luo M.-F., and Wang B.-P. Effects of organic chemicals on growth of Methylosinus trichosporium OB3b. Biochem. Eng. J. 31 (2006) 113-117
212. Yoch D.C., Chen Y.P., and Hardin M.G. Formate dehydrogenase from the methane-oxidizer Methylosinus trichosporium OB3b. J. Bacteriol. 172 (1990) 4456-4463
213. Yu S.S.-F., Chen K.H.-C., Tseng M.Y.-H., Wang Y.-S., Tseng C.-H., Chen Y.-J., Huang D.-S., and 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. 185 (2003) 5915-5924
214. Zahn J.A., Bergmann D.J., Boyd J.M., Kunz R.C., and DiSpirito A.A. Membrane-associated quinoprotein formaldehyde dehydrogenase from Methylococcus capsulatus (Bath). J. Bacteriol. 183 (2001) 6832-6840
215. Zhang M., and Lidstrom M.E. Promoters and transcripts for genes involved in methanol oxidation in Methylobacterium extorquens AM1. Microbiology 149 (2003) 1033-1040