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1 in detail for the soluble form of the enzyme methane monooxygenase.
2 for the high-valent diiron intermediate Q of methane monooxygenase.
3 edium and expressing the membrane-associated methane monooxygenase.
4 low-copper medium and expressing the soluble methane monooxygenase.
5 phs contain both a soluble and a 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 d to be enabled by expression of the soluble methane monooxygenase.
9 ite resembling the Cu(B) site in particulate methane monooxygenase.
10 their primary metabolic enzyme, particulate methane monooxygenase.
11 copper for the membrane-bound (particulate) methane monooxygenase.
12 e cytosol, and stores copper for particulate methane monooxygenase.
13 at the dicopper site within the particulate methane monooxygenase.
14 core proposed for intermediate Q of soluble methane monooxygenase.
15 cies, T201S(peroxo), similar to H(peroxo) in methane monooxygenase.
16 ne gas fluxes to inform microcosms targeting methane monooxygenase activity and its potential role in
18 n hemerythrin, ribonucleotide reductase, and methane monooxygenase, all of which can bind NO and O2.
19 This finding differs from that with soluble methane monooxygenase and cytochrome P-450 monooxygenase
20 alytic hydrocarbon oxidations by particulate methane monooxygenase and heterogeneous zeolite systems.
21 ral information on the multicomponent enzyme methane monooxygenase and its components: a hydroxylase
23 the dioxygen activation reactions in soluble methane monooxygenase and related carboxylate-bridged di
24 e fold and is distinct from those of soluble methane monooxygenase and related enzymes that utilize a
26 its more extensively studied members such as methane monooxygenase and stearoyl acyl carrier protein
27 ers of ribonucleotide reductase, the soluble methane monooxygenase, and the stearoyl-ACP delta 9 desa
29 gulates the metabolic switch between the two methane monooxygenases but also regulates the level of e
31 observed in the NMR structures of T4moD, the methane monooxygenase effector protein (MmoB) from two m
32 structure of T4moD is closer to that of the methane monooxygenase effector protein from M. capsulatu
33 Although the published NMR structures of the methane monooxygenase effector proteins from Methylosinu
34 he presence of a particulate, membrane-bound methane monooxygenase enzyme in M. silvestris BL2 and th
37 es copper for the regulation and activity of methane monooxygenase enzymes, experimental data for dir
38 ties of the hydroxylase component of soluble methane monooxygenase from Methylococcus capsulatus (Bat
39 nce our current understanding of particulate methane monooxygenase function by the characterization o
41 del the diiron(IV) intermediate Q of soluble methane monooxygenase have led to the synthesis of a dii
45 nd substituted methanes by intermediate Q in methane monooxygenase hydroxylase (MMOH) has been quanti
46 trates, methane and dioxygen, in the soluble methane monooxygenase hydroxylase (MMOH), we determined
51 carried out by iron centres-such as that of methane monooxygenase in methane hydroxylation-through d
52 s shown to be susceptible to the particulate methane monooxygenase inhibitor 1,7-octadiyne and a bact
54 Q, the methane-oxidizing species of soluble methane monooxygenase, is proposed to have an [Fe(IV)(2)
55 he reductase component (MMOR) of the soluble methane monooxygenase isolated from Methylosinus trichos
56 re able to selectively oxidize methane using methane monooxygenase (MMO) and methyl coenzyme M reduct
58 iates of the Methylosinus trichosporium OB3b methane monooxygenase (MMO) catalytic cycle are studied
62 uced hydroxylase component (MMOH) of soluble methane monooxygenase (MMO) from Methylosinus trichospor
63 erved in nature, which is surprising because methane monooxygenase (MMO) gene expression has been une
67 ion process catalyzed by the soluble form of methane monooxygenase (MMO) isolated from Methylosinus t
69 ein effects in the activation of dioxygen by methane monooxygenase (MMO) were investigated by using c
70 n activation is required for enzymes such as methane monooxygenase (MMO), for which catalysis depends
71 n other diiron carboxylate proteins, such as methane monooxygenase (MMO), the R2 diiron cluster is pr
75 ters in the hydroxylase component of soluble methane monooxygenase (MMOH) and in the D84E mutant of t
76 tion by the hydroxylase component of soluble methane monooxygenase (MMOH) is determined to atomic det
78 ersion to methanol under mild conditions are methane monooxygenases (MMOs) found in methanotrophic ba
80 metabolic pathway, aerobic methanotrophs use methane monooxygenases (MMOs) to activate methane, oxidi
84 vealed that the structural genes for soluble methane monooxygenase, mmoXYBZDC, were adjacent to two g
85 r iron centre similar to that in the soluble methane monooxygenases of methanotrophic bacteria, to wh
86 ed either by expression of the two different methane monooxygenases or by addition of ammonia to the
87 that have been detected in the reactions of methane monooxygenase (P or H(peroxo)) and variants of R
88 ations of methane to methanol by particulate methane monooxygenase (pMMO) and ammonia to hydroxylamin
89 n of the putative active site of particulate methane monooxygenase (pMMO) and polysaccharide monooxyg
92 in the MALDI-MS analysis of the particulate methane monooxygenase (pMMO) complex, a three-subunit tr
93 thane oxidation using the enzyme particulate methane monooxygenase (pMMO) contributes to the removal
94 ctive preparation of the membrane-associated methane monooxygenase (pMMO) from Methylococcus capsulat
95 found that DPI inhibits both membrane-bound methane monooxygenase (pMMO) from Methylococcus capsulat
96 ined for the type 2 Cu2+ site in particulate methane monooxygenase (pMMO) from Methylomicrobium album
97 itecture of the copper-dependent particulate methane monooxygenase (pMMO) have been investigated exte
98 ments in purification of membrane-associated methane monooxygenase (pMMO) have resulted in preparatio
99 e two gene clusters encoding the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus
108 ers where genes encoding for the particulate methane monooxygenase (pMMO) were transcribed by a novel
109 lenging reaction is catalyzed by particulate methane monooxygenase (pMMO), a copper-dependent integra
110 ethane oxidation is catalyzed by particulate methane monooxygenase (pMMO), a copper-dependent, membra
111 izing enzyme, the membrane-bound particulate methane monooxygenase (pMMO), catalyzes the oxidation of
112 abolic enzyme of these bacteria, particulate methane monooxygenase (pMMO), has been controversial owi
114 Their primary metabolic enzyme, particulate methane monooxygenase (pMMO), is housed in copper-induce
115 hanotrophs require Cu to sustain particulate methane monooxygenase (pMMO), the most efficient enzyme
122 red on detection of 16S rRNA and particulate methane monooxygenase (pmoA) genes for two putative aero
127 of functions; proteins in this class include methane monooxygenase, ribonucleotide reductase, Delta(9
128 (two-component electron transfer scheme) and methane monooxygenase (small regulatory protein and diir
129 ds by nonheme diiron enzymes such as soluble methane monooxygenase (sMMO) and fatty acid desaturases.
130 of the catalytic sites in two MMOs: soluble methane monooxygenase (sMMO) and particulate methane mon
131 l by two enzymes, the iron-dependent soluble methane monooxygenase (sMMO) and the copper-dependent pa
132 ifferent enzymes, the cytoplasmic or soluble methane monooxygenase (sMMO) and the membrane-bound or p
133 ated in medium with cells expressing soluble methane monooxygenase (sMMO) and then monitored for morp
134 applied to the diiron active site of soluble methane monooxygenase (sMMO) and to a series of high-val
140 ic cytochome P450 enzymes and by the soluble methane monooxygenase (sMMO) enzyme from Methylococcusca
142 opped-flow kinetic investigations of soluble methane monooxygenase (sMMO) from M. capsulatus (Bath) h
146 nism of hydrocarbon oxidation by the soluble methane monooxygenase (sMMO) from Methylococcus capsulat
147 on the hydroxylase of a BMM enzyme, soluble methane monooxygenase (sMMO) from Methylococcus capsulat
148 and three diiron-containing enzymes, soluble methane monooxygenase (sMMO) from Methylococcus capsulat
149 2E1 T303A, and three diiron enzymes, soluble methane monooxygenase (sMMO) from Methylococcus capsulat
151 region of the B component (MMOB) of soluble methane monooxygenase (sMMO) from Methylosinus trichospo
152 The regulatory component (MMOB) of soluble methane monooxygenase (sMMO) has a unique N-terminal tai
154 The regulatory component MMOB of soluble methane monooxygenase (sMMO) has been hypothesized to co
157 to both the H(mv) and H(ox) forms of soluble methane monooxygenase (sMMO) in solution has been studie
161 lase component (MMOH) of the soluble form of methane monooxygenase (sMMO) isolated from Methylosinus
162 the hydroxylase component (MMOH) of soluble methane monooxygenase (sMMO) primes its non-heme diiron
163 onas butanovora has high homology to soluble methane monooxygenase (sMMO), and both oxidize a wide ra
164 rmed by the hydroxylase component of soluble methane monooxygenase (sMMO), as proposed previously on
165 s involved in the catalytic cycle of soluble methane monooxygenase (sMMO), the enzyme that selectivel
170 een postulated for intermediate Q of soluble methane monooxygenase (sMMO-Q), the oxidant responsible
173 oth the wild type and a constitutive soluble methane monooxygenase (sMMOC) mutant, PP319, of Methylos
174 ly characterized in the reactions of soluble methane monooxygenase, stearoyl acyl carrier protein Del
175 ch as hemerythrin, ribonucleotide reductase, methane monooxygenase, stearoyl-acyl carrier protein (AC
180 analogous to that of the methanotroph enzyme methane monooxygenase that activates methane at ambient
181 robic growth on methane, including a soluble methane monooxygenase that catalyses the hydroxylation o
182 atically critical subunit of the particulate methane monooxygenase, the predominant methane oxidation
183 M. gorgona MG08 encodes a single particulate methane monooxygenase, the serine cycle for assimilation
185 switch to using the iron-containing soluble methane monooxygenase to catalyse methane oxidation, wit
186 vity of the methane-oxidizing enzyme soluble methane monooxygenase under conditions where bioavailabl
187 e methane is oxidized to methanol by soluble methane monooxygenase via a diiron(IV) intermediate call
190 nd reactivity of active sites in particulate methane monooxygenase, which are enzymes able to selecti
191 p in both of these processes is catalyzed by methane monooxygenase, which converts methane or ammonia
192 ted by ethyne, a potent inhibitor of soluble methane monooxygenase with which alkene monooxygenase sh