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1 interactions between aerobic methanotrophs (Methylococcus and Methylocystis) and perchlorate-reducin
2 domain, is typified by the DmcR protein from Methylococcus and the other by the PocR protein of Salmo
3 eiphilum (a betaproteobacterium, 4 Mbp), and Methylococcus capsulatus (a gammaproteobacterium, 3.3 Mb
6 report a cyro-EM structure of holo-pMMO from Methylococcus capsulatus (Bath) at 2.5 A, and develop qu
8 he soluble methane monooxygenase system from Methylococcus capsulatus (Bath) catalyzes the oxidation
10 determined the X-ray structures of MMOH from Methylococcus capsulatus (Bath) cocrystallized with dibr
11 dical clock substrate, catalyzed by MMO from Methylococcus capsulatus (Bath) gave only cubylmethanol
12 lated proteins have been identified, and the Methylococcus capsulatus (Bath) genome has been sequence
13 ins from Methylosinus trichosporium OB3b and Methylococcus capsulatus (Bath) have a similar secondary
14 ponent of soluble methane monooxygenase from Methylococcus capsulatus (Bath) have been thoroughly inv
15 ethane monooxygenase hydroxylase (MMOH) from Methylococcus capsulatus (Bath) in frozen 4:1 buffer/gly
16 report here crystal structures of MMOH from Methylococcus capsulatus (Bath) in the diiron(II), diiro
17 The soluble methane monooxygenase system of Methylococcus capsulatus (Bath) includes three protein c
18 he soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) is a multicomponent enzy
19 Soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) is a three-component enz
20 O; EC 1.14.13.25) from the pseudothermophile Methylococcus capsulatus (Bath) is a three-component enz
22 activity assays on membrane-bound pMMO from Methylococcus capsulatus (Bath) reveal that zinc inhibit
25 the structure of pMMO from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8 A
27 e methane monooxygenase (sMMO) isolated from Methylococcus capsulatus (Bath) utilizes a carboxylate-b
29 Several strains of methanotrophs, including Methylococcus capsulatus (Bath), express a membrane-boun
30 s, soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath), toluene monooxygenase (
31 s, soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath), toluene monooxygenase (
37 rane-bound methane monooxygenase (pMMO) from Methylococcus capsulatus and ammonia monooxygenase (AMO)
39 particulate methane monooxygenase (pMMO) in Methylococcus capsulatus Bath was assessed by analysis o
40 associated methane monooxygenase (pMMO) from Methylococcus capsulatus Bath was isolated by ion-exchan
47 nthetic pathway were in the proteobacterium, Methylococcus capsulatus, in which sterol biosynthesis i