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1  RT-PCR expression assays were developed for Methylosinus trichosporium OB3b (which produces mb) to q
2 ly of bacterial copper storage proteins from Methylosinus trichosporium OB3b and Bacillus subtilis.
3 methane monooxygenase effector proteins from Methylosinus trichosporium OB3b and Methylococcus capsul
4  may be present in the type II methanotrophs Methylosinus trichosporium OB3b and Methylocystis parvus
5 6- and 99-base regions of the pmoA gene from Methylosinus trichosporium OB3b and Methylomicrobium alb
6 f methane monooxygenase (sMMO) isolated from Methylosinus trichosporium OB3b catalyzes both the O2 ac
7    Soluble methane monooxygenase (sMMO) from Methylosinus trichosporium OB3b catalyzes the oxidation
8  soluble methane monooxygenase isolated from Methylosinus trichosporium OB3b catalyzes transfer of 2e
9 of methane monooxygenase (MMO) isolated from Methylosinus trichosporium OB3b have been studied.
10                                    MMOB from Methylosinus trichosporium OB3b is devoid of cysteine.
11 y of the reaction cycle intermediates of the Methylosinus trichosporium OB3b methane monooxygenase (M
12            Both of the histidine residues in Methylosinus trichosporium OB3b MMOB (H5 and H33) were c
13 of soluble methane monooxygenase (sMMO) from Methylosinus trichosporium OB3b on steady-state turnover
14  of soluble methane monooxygenase (MMO) from Methylosinus trichosporium OB3b reacts with O2 and CH4 t
15 storage protein (Csp1) from the methanotroph Methylosinus trichosporium OB3b that is exported from th
16 ubane with the reconstituted MMO system from Methylosinus trichosporium OB3b yields both cubylmethano
17 ected to encode for this precursor, mbnA, in Methylosinus trichosporium OB3b, abolishes methanobactin
18 eptide from the methane-oxidizing bacterium, Methylosinus trichosporium OB3b, believed to be involved
19                 pMMO from a second organism, Methylosinus trichosporium OB3b, has been purified and c
20 copper chelator produced by the methanotroph Methylosinus trichosporium OB3b, is hypothesized to medi
21  component of a copper acquisition system in Methylosinus trichosporium OB3b, the metal binding prope
22 of methanobactin (MB), a peptide produced by Methylosinus trichosporium OB3b, which has an exceptiona
23 e (C45N12O14H62Cu, 1216 daltons) produced by Methylosinus trichosporium OB3b.
24 hane monooxygenase (sMMOC) mutant, PP319, of Methylosinus trichosporium OB3b.
25 positions, than the characterized mbtin from Methylosinus trichosporium OB3b.

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