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MeSH Review

Methylosinus

 
 
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Disease relevance of Methylosinus

  • The methanotrophic bacteria Methylococcus capsulatus (Bath) and Methylosinus trichosporium OB3b convert methane to methanol using the enzyme, methane monooxygenase (MMO) [1].
  • The site preferences produced during hydroxylamine oxidation were 33.5 +/- 1.2 per thousand, 32.5 +/- 0.6 per thousand, and 35.6 +/- 1.4 per thousand for Nitrosomonas europaea, Nitrosospira multiformis, and Methylosinus trichosporium, respectively, indicating similar site preferences for methane and ammonia oxidizers [2].
  • Kinetics of chlorinated hydrocarbon degradation by Methylosinus trichosporium OB3b and toxicity of trichloroethylene [3].
  • Ammonia switch-off of nitrogenase from Rhodobacter sphaeroides and Methylosinus trichosporium: no evidence for Fe protein modification [4].
  • For reference, nifH and nifD sequences were also obtained from some type II MB of the alphaproteobacterial Methylosinus/Methylocystis group and from gammaproteobacterial type I MB [5].
 

High impact information on Methylosinus

  • The methanotrophic bacterium Methylosinus trichosporium 0B3b degrades trichloroethylene more rapidly than other bacteria examined to date [6].
  • Formate dehydrogenase from Methylosinus trichosporium OB3b. Purification and spectroscopic characterization of the cofactors [7].
  • Soluble methane monooxygenase (sMMO) from Methylosinus trichosporium OB3b catalyzes the oxidation of norcarane to afford 3-hydroxymethylcyclohexene and 3-cycloheptenol, compounds characteristic of radical and cationic intermediates, respectively, in addition to 2- and 3-norcaranols [8].
  • The hydroxylase component (MMOH) of the soluble form of methane monooxygenase (sMMO) isolated from Methylosinus trichosporium OB3b catalyzes both the O2 activation and the CH4 oxidation reactions at the oxygen-bridged dinuclear iron cluster present in its buried active site [9].
  • Spectral, kinetic, and thermodynamic properties of Cu(I) and Cu(II) binding by methanobactin from Methylosinus trichosporium OB3b [10].
 

Chemical compound and disease context of Methylosinus

  • The reduced hydroxylase component (MMOH) of soluble methane monooxygenase (MMO) from Methylosinus trichosporium OB3b reacts with O2 and CH4 to produce CH3OH and H2O in a single-turnover reaction [11].
  • 2. Contrary to previous reports, NAD(P)H and not ascorbate is the required electron donor for the enzyme from Methylosinus trichosporium [12].
  • Both of the histidine residues in Methylosinus trichosporium OB3b MMOB (H5 and H33) were chemically modified by diethylpyrocarbonate (DEPC) [13].
  • MMOB from Methylosinus trichosporium OB3b is devoid of cysteine [14].
  • Inhibition of dimethyl ether and methane oxidation in Methylococcus capsulatus and Methylosinus trichosporium [15].
 

Biological context of Methylosinus

 

Gene context of Methylosinus

  • The gene encoding a soluble MMO component B protein from Methylosinus trichosporium OB3b was cloned [17].
  • The microbial degradation of chlorinated and nonchlorinated methanes, ethanes, and ethanes by a mixed methane-oxidizing culture grown under chemostat and batch conditions is evaluated and compared with that by two pure methanotrophic strains: CAC1 (isolated from the mixed culture) and Methylosinus trichosporium OB3b [18].
  • However, unlike other Type II methanotrophs, it appeared that glutamine synthetase activity was regulated by adenylylation in this organism. 'Methylosinus' 6 was grown in continuous culture with either dinitrogen or nitrate as sole nitrogen source under various dissolved oxygen tensions [19].
 

Analytical, diagnostic and therapeutic context of Methylosinus

  • It was concluded that a type II methanotrophic bacterium phylogenetically related to Methylosinus species synthesizes soluble methane monooxygenase and is responsible for trichloroethylene oxidation in the bioreactor [20].

References

  1. Copper-dependent reciprocal transcriptional regulation of methane monooxygenase genes in Methylococcus capsulatus and Methylosinus trichosporium. Nielsen, A.K., Gerdes, K., Murrell, J.C. Mol. Microbiol. (1997) [Pubmed]
  2. Distinguishing nitrous oxide production from nitrification and denitrification on the basis of isotopomer abundances. Sutka, R.L., Ostrom, N.E., Ostrom, P.H., Breznak, J.A., Gandhi, H., Pitt, A.J., Li, F. Appl. Environ. Microbiol. (2006) [Pubmed]
  3. Kinetics of chlorinated hydrocarbon degradation by Methylosinus trichosporium OB3b and toxicity of trichloroethylene. Oldenhuis, R., Oedzes, J.Y., van der Waarde, J.J., Janssen, D.B. Appl. Environ. Microbiol. (1991) [Pubmed]
  4. Ammonia switch-off of nitrogenase from Rhodobacter sphaeroides and Methylosinus trichosporium: no evidence for Fe protein modification. Yoch, D.C., Li, J.D., Hu, C.Z., Scholin, C. Arch. Microbiol. (1988) [Pubmed]
  5. NifH and NifD phylogenies: an evolutionary basis for understanding nitrogen fixation capabilities of methanotrophic bacteria. Dedysh, S.N., Ricke, P., Liesack, W. Microbiology (Reading, Engl.) (2004) [Pubmed]
  6. Biodegradation of low-molecular-weight halogenated hydrocarbons by methanotrophic bacteria. Hanson, R.S., Tsien, H.C., Tsuji, K., Brusseau, G.A., Wackett, L.P. FEMS Microbiol. Rev. (1990) [Pubmed]
  7. Formate dehydrogenase from Methylosinus trichosporium OB3b. Purification and spectroscopic characterization of the cofactors. Jollie, D.R., Lipscomb, J.D. J. Biol. Chem. (1991) [Pubmed]
  8. Intermediate Q from soluble methane monooxygenase hydroxylates the mechanistic substrate probe norcarane: evidence for a stepwise reaction. Brazeau, B.J., Austin, R.N., Tarr, C., Groves, J.T., Lipscomb, J.D. J. Am. Chem. Soc. (2001) [Pubmed]
  9. Regulation of methane monooxygenase catalysis based on size exclusion and quantum tunneling. Zheng, H., Lipscomb, J.D. Biochemistry (2006) [Pubmed]
  10. Spectral, kinetic, and thermodynamic properties of Cu(I) and Cu(II) binding by methanobactin from Methylosinus trichosporium OB3b. Choi, D.W., Zea, C.J., Do, Y.S., Semrau, J.D., Antholine, W.E., Hargrove, M.S., Pohl, N.L., Boyd, E.S., Geesey, G.G., Hartsel, S.C., Shafe, P.H., McEllistrem, M.T., Kisting, C.J., Campbell, D., Rao, V., de la Mora, A.M., Dispirito, A.A. Biochemistry (2006) [Pubmed]
  11. Large kinetic isotope effects in methane oxidation catalyzed by methane monooxygenase: evidence for C-H bond cleavage in a reaction cycle intermediate. Nesheim, J.C., Lipscomb, J.D. Biochemistry (1996) [Pubmed]
  12. A comparison of the substrate and electron-donor specificities of the methane mono-oxygenases from three strains of methane-oxidizing bacteria. Stirling, D.I., Colby, J., Dalton, H. Biochem. J. (1979) [Pubmed]
  13. Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle. Wallar, B.J., Lipscomb, J.D. Biochemistry (2001) [Pubmed]
  14. Methane monooxygenase hydroxylase and B component interactions. Zhang, J., Wallar, B.J., Popescu, C.V., Renner, D.B., Thomas, D.D., Lipscomb, J.D. Biochemistry (2006) [Pubmed]
  15. Inhibition of dimethyl ether and methane oxidation in Methylococcus capsulatus and Methylosinus trichosporium. Patel, R., Hou, C.T., Felix, A. J. Bacteriol. (1976) [Pubmed]
  16. Purification, crystallisation and preliminary X-ray diffraction characterisation of methanol dehydrogenase from Methylosinus trichosporium OB3b. Parker, M.W., Cornish, A., Gossain, V., Best, D.J. Eur. J. Biochem. (1987) [Pubmed]
  17. Soluble methane monooxygenase component B gene probe for identification of methanotrophs that rapidly degrade trichloroethylene. Tsien, H.C., Hanson, R.S. Appl. Environ. Microbiol. (1992) [Pubmed]
  18. Biodegradation of individual and multiple chlorinated aliphatic hydrocarbons by methane-oxidizing cultures. Chang, H.L., Alvarez-Cohen, L. Appl. Environ. Microbiol. (1996) [Pubmed]
  19. Nitrogen metabolism in a new obligate methanotroph, 'Methylosinus' strain 6. Toukdarian, A.E., Lidstrom, M.E. J. Gen. Microbiol. (1984) [Pubmed]
  20. Characterization of a methane-utilizing bacterium from a bacterial consortium that rapidly degrades trichloroethylene and chloroform. Alvarez-Cohen, L., McCarty, P.L., Boulygina, E., Hanson, R.S., Brusseau, G.A., Tsien, H.C. Appl. Environ. Microbiol. (1992) [Pubmed]
 
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