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1 domain, is typified by the DmcR protein from Methylococcus and the other by the PocR protein of Salmo
2 eiphilum (a betaproteobacterium, 4 Mbp), and Methylococcus capsulatus (a gammaproteobacterium, 3.3 Mb
6 he soluble methane monooxygenase system from Methylococcus capsulatus (Bath) catalyzes the oxidation
8 determined the X-ray structures of MMOH from Methylococcus capsulatus (Bath) cocrystallized with dibr
9 dical clock substrate, catalyzed by MMO from Methylococcus capsulatus (Bath) gave only cubylmethanol
10 lated proteins have been identified, and the Methylococcus capsulatus (Bath) genome has been sequence
11 ins from Methylosinus trichosporium OB3b and Methylococcus capsulatus (Bath) have a similar secondary
12 ponent of soluble methane monooxygenase from Methylococcus capsulatus (Bath) have been thoroughly inv
13 ethane monooxygenase hydroxylase (MMOH) from Methylococcus capsulatus (Bath) in frozen 4:1 buffer/gly
14 report here crystal structures of MMOH from Methylococcus capsulatus (Bath) in the diiron(II), diiro
15 The soluble methane monooxygenase system of Methylococcus capsulatus (Bath) includes three protein c
16 he soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) is a multicomponent enzy
17 Soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) is a three-component enz
18 O; EC 1.14.13.25) from the pseudothermophile Methylococcus capsulatus (Bath) is a three-component enz
20 activity assays on membrane-bound pMMO from Methylococcus capsulatus (Bath) reveal that zinc inhibit
23 the structure of pMMO from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8 A
25 e methane monooxygenase (sMMO) isolated from Methylococcus capsulatus (Bath) utilizes a carboxylate-b
26 Several strains of methanotrophs, including Methylococcus capsulatus (Bath), express a membrane-boun
27 s, soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath), toluene monooxygenase (
28 s, soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath), toluene monooxygenase (
34 rane-bound methane monooxygenase (pMMO) from Methylococcus capsulatus and ammonia monooxygenase (AMO)
36 particulate methane monooxygenase (pMMO) in Methylococcus capsulatus Bath was assessed by analysis o
37 associated methane monooxygenase (pMMO) from Methylococcus capsulatus Bath was isolated by ion-exchan
43 nthetic pathway were in the proteobacterium, Methylococcus capsulatus, in which sterol biosynthesis i
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