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1 for the high-valent diiron intermediate Q of methane monooxygenase.
2 edium and expressing the membrane-associated methane monooxygenase.
3 low-copper medium and expressing the soluble methane monooxygenase.
4 phs contain both a soluble and a particulate methane monooxygenase.
5 copper for the membrane-bound (particulate) methane monooxygenase.
6 ound in the hydroxylase component of soluble methane monooxygenase.
7 ge(s) in the diferric state, as observed for methane monooxygenase.
8 e cytosol, and stores copper for particulate methane monooxygenase.
9 at the dicopper site within the particulate methane monooxygenase.
10 core proposed for intermediate Q of soluble methane monooxygenase.
11 cies, T201S(peroxo), similar to H(peroxo) in methane monooxygenase.
13 n hemerythrin, ribonucleotide reductase, and methane monooxygenase, all of which can bind NO and O2.
14 This finding differs from that with soluble methane monooxygenase and cytochrome P-450 monooxygenase
15 alytic hydrocarbon oxidations by particulate methane monooxygenase and heterogeneous zeolite systems.
16 ral information on the multicomponent enzyme methane monooxygenase and its components: a hydroxylase
17 the dioxygen activation reactions in soluble methane monooxygenase and related carboxylate-bridged di
18 e fold and is distinct from those of soluble methane monooxygenase and related enzymes that utilize a
20 its more extensively studied members such as methane monooxygenase and stearoyl acyl carrier protein
21 ers of ribonucleotide reductase, the soluble methane monooxygenase, and the stearoyl-ACP delta 9 desa
23 gulates the metabolic switch between the two methane monooxygenases but also regulates the level of e
24 observed in the NMR structures of T4moD, the methane monooxygenase effector protein (MmoB) from two m
25 structure of T4moD is closer to that of the methane monooxygenase effector protein from M. capsulatu
26 Although the published NMR structures of the methane monooxygenase effector proteins from Methylosinu
27 he presence of a particulate, membrane-bound methane monooxygenase enzyme in M. silvestris BL2 and th
29 es copper for the regulation and activity of methane monooxygenase enzymes, experimental data for dir
30 ties of the hydroxylase component of soluble methane monooxygenase from Methylococcus capsulatus (Bat
31 nce our current understanding of particulate methane monooxygenase function by the characterization o
33 del the diiron(IV) intermediate Q of soluble methane monooxygenase have led to the synthesis of a dii
37 nd substituted methanes by intermediate Q in methane monooxygenase hydroxylase (MMOH) has been quanti
38 trates, methane and dioxygen, in the soluble methane monooxygenase hydroxylase (MMOH), we determined
43 carried out by iron centres-such as that of methane monooxygenase in methane hydroxylation-through d
45 Q, the methane-oxidizing species of soluble methane monooxygenase, is proposed to have an [Fe(IV)(2)
46 he reductase component (MMOR) of the soluble methane monooxygenase isolated from Methylosinus trichos
47 re able to selectively oxidize methane using methane monooxygenase (MMO) and methyl coenzyme M reduct
49 iates of the Methylosinus trichosporium OB3b methane monooxygenase (MMO) catalytic cycle are studied
52 uced hydroxylase component (MMOH) of soluble methane monooxygenase (MMO) from Methylosinus trichospor
53 erved in nature, which is surprising because methane monooxygenase (MMO) gene expression has been une
57 ion process catalyzed by the soluble form of methane monooxygenase (MMO) isolated from Methylosinus t
59 ein effects in the activation of dioxygen by methane monooxygenase (MMO) were investigated by using c
60 n activation is required for enzymes such as methane monooxygenase (MMO), for which catalysis depends
61 n other diiron carboxylate proteins, such as methane monooxygenase (MMO), the R2 diiron cluster is pr
66 ters in the hydroxylase component of soluble methane monooxygenase (MMOH) and in the D84E mutant of t
67 tion by the hydroxylase component of soluble methane monooxygenase (MMOH) is determined to atomic det
69 ersion to methanol under mild conditions are methane monooxygenases (MMOs) found in methanotrophic ba
74 vealed that the structural genes for soluble methane monooxygenase, mmoXYBZDC, were adjacent to two g
75 r iron centre similar to that in the soluble methane monooxygenases of methanotrophic bacteria, to wh
76 ed either by expression of the two different methane monooxygenases or by addition of ammonia to the
77 that have been detected in the reactions of methane monooxygenase (P or H(peroxo)) and variants of R
78 n of the putative active site of particulate methane monooxygenase (pMMO) and polysaccharide monooxyg
81 in the MALDI-MS analysis of the particulate methane monooxygenase (pMMO) complex, a three-subunit tr
82 ctive preparation of the membrane-associated methane monooxygenase (pMMO) from Methylococcus capsulat
83 found that DPI inhibits both membrane-bound methane monooxygenase (pMMO) from Methylococcus capsulat
84 ined for the type 2 Cu2+ site in particulate methane monooxygenase (pMMO) from Methylomicrobium album
85 ments in purification of membrane-associated methane monooxygenase (pMMO) have resulted in preparatio
86 e two gene clusters encoding the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus
94 lenging reaction is catalyzed by particulate methane monooxygenase (pMMO), a copper-dependent integra
95 hanotrophs require Cu to sustain particulate methane monooxygenase (pMMO), the most efficient enzyme
101 red on detection of 16S rRNA and particulate methane monooxygenase (pmoA) genes for two putative aero
106 of functions; proteins in this class include methane monooxygenase, ribonucleotide reductase, Delta(9
107 (two-component electron transfer scheme) and methane monooxygenase (small regulatory protein and diir
108 of the catalytic sites in two MMOs: soluble methane monooxygenase (sMMO) and particulate methane mon
109 ifferent enzymes, the cytoplasmic or soluble methane monooxygenase (sMMO) and the membrane-bound or p
110 ated in medium with cells expressing soluble methane monooxygenase (sMMO) and then monitored for morp
111 applied to the diiron active site of soluble methane monooxygenase (sMMO) and to a series of high-val
116 ic cytochome P450 enzymes and by the soluble methane monooxygenase (sMMO) enzyme from Methylococcusca
118 opped-flow kinetic investigations of soluble methane monooxygenase (sMMO) from M. capsulatus (Bath) h
120 nism of hydrocarbon oxidation by the soluble methane monooxygenase (sMMO) from Methylococcus capsulat
121 on the hydroxylase of a BMM enzyme, soluble methane monooxygenase (sMMO) from Methylococcus capsulat
122 and three diiron-containing enzymes, soluble methane monooxygenase (sMMO) from Methylococcus capsulat
123 2E1 T303A, and three diiron enzymes, soluble methane monooxygenase (sMMO) from Methylococcus capsulat
127 region of the B component (MMOB) of soluble methane monooxygenase (sMMO) from Methylosinus trichospo
128 The regulatory component (MMOB) of soluble methane monooxygenase (sMMO) has a unique N-terminal tai
129 The regulatory component MMOB of soluble methane monooxygenase (sMMO) has been hypothesized to co
132 to both the H(mv) and H(ox) forms of soluble methane monooxygenase (sMMO) in solution has been studie
135 lase component (MMOH) of the soluble form of methane monooxygenase (sMMO) isolated from Methylosinus
136 the hydroxylase component (MMOH) of soluble methane monooxygenase (sMMO) primes its non-heme diiron
137 onas butanovora has high homology to soluble methane monooxygenase (sMMO), and both oxidize a wide ra
138 rmed by the hydroxylase component of soluble methane monooxygenase (sMMO), as proposed previously on
141 een postulated for intermediate Q of soluble methane monooxygenase (sMMO-Q), the oxidant responsible
143 oth the wild type and a constitutive soluble methane monooxygenase (sMMOC) mutant, PP319, of Methylos
144 ly characterized in the reactions of soluble methane monooxygenase, stearoyl acyl carrier protein Del
145 ch as hemerythrin, ribonucleotide reductase, methane monooxygenase, stearoyl-acyl carrier protein (AC
151 switch to using the iron-containing soluble methane monooxygenase to catalyse methane oxidation, wit
152 e methane is oxidized to methanol by soluble methane monooxygenase via a diiron(IV) intermediate call
155 nd reactivity of active sites in particulate methane monooxygenase, which are enzymes able to selecti
156 ted by ethyne, a potent inhibitor of soluble methane monooxygenase with which alkene monooxygenase sh
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