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

• Methanol dehydrogenase was purified from the obligate methanotroph, Methylosinus trichosporium OB3b, in two steps from disrupted biomass by aqueous two-phase partition and ion-exchange chromatography [16].

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