1.14.13.25: methane monooxygenase (soluble)
This is an abbreviated version!
For detailed information about methane monooxygenase (soluble), go to the full flat file.
Word Map on EC 1.14.13.25
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1.14.13.25
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methanotrophs
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methanol
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methylosinus
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capsulatus
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methylococcus
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trichosporium
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methane-oxidizing
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methylocystis
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ch4
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methylomonas
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dioxygen
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dinuclear
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methylobacter
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trichloroethylene
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methylomicrobium
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alkane
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diironii
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ammonia-oxidizing
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landfill
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upland
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antiferromagnetically
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wetland
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high-valent
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non-motile
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copper-containing
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carboxylate-bridged
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peat
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copper-dependent
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dicopper
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ch3oh
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nitrosomonas
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cometabolic
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diferrous
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methanobactins
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energy production
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mixed-valent
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gammaproteobacterial
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sphagnum
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t-rflp
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seep
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propene
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synthesis
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biotechnology
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degradation
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exafs
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nitrify
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peroxo
- 1.14.13.25
- methanotrophs
- methanol
- methylosinus
- capsulatus
- methylococcus
- trichosporium
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methane-oxidizing
- methylocystis
- ch4
- methylomonas
- dioxygen
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dinuclear
- methylobacter
- trichloroethylene
- methylomicrobium
- alkane
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diironii
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ammonia-oxidizing
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landfill
-
upland
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antiferromagnetically
-
wetland
-
high-valent
-
non-motile
-
copper-containing
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carboxylate-bridged
-
peat
-
copper-dependent
-
dicopper
- ch3oh
- nitrosomonas
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cometabolic
-
diferrous
-
methanobactins
- energy production
-
mixed-valent
-
gammaproteobacterial
- sphagnum
-
t-rflp
-
seep
- propene
- synthesis
- biotechnology
- degradation
-
exafs
-
nitrify
-
peroxo
Reaction
Synonyms
chcA, cytoplasmic methane monooxygenase, methane hydroxylase, methane mono-oxygenase, methane monooxygenase, methane monooxygenase hydroxylase, MmMmoC, MMO, MMO Bath, MMOB, MmoC, MMOH, MMOR, oxygenase, methane mono-, particulate methane monooxygenase, pMMO, sMMO, soluble methane monooxygenase, soluble methane monooxygenase hydroxylase
ECTree
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Subunits
Subunits on EC 1.14.13.25 - methane monooxygenase (soluble)
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dimer
heterotrimer
hexamer
trimer
additional information
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component A: 2 * 55000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
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protein A: 2 * 54000-60630, alpha+ 2 * 42000-44720, beta + 2 * 17000-19840, gamma
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component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
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the hydroxylase (MMOH) component is a homodimer that consists of two protomers, and each protomer has three polypeptides (alphabetagamma), 60600 (alpha/MmoX) + 40500 (beta/MmoY) + 19800 (gamma/MmoZ), two equivalent of the regulatory component (MmoB) bind to one equivalent MMOH (alpha2beta2gamma2), + reductase protein (MmoC), + 12000 (MmoD)
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protein A: 2 * 54000-60630, alpha+ 2 * 42000-44720, beta + 2 * 17000-19840, gamma
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component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
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Methylococcus capsulatus Bath.
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the hydroxylase (MMOH) component is a homodimer that consists of two protomers, and each protomer has three polypeptides (alphabetagamma), 60600 (alpha/MmoX) + 40500 (beta/MmoY) + 19800 (gamma/MmoZ), two equivalent of the regulatory component (MmoB) bind to one equivalent MMOH (alpha2beta2gamma2), + reductase protein (MmoC), + 12000 (MmoD)
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component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
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component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
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component A: 2 * 56000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
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component A: 2 * 56000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
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component A: 2 * 54400 alpha, 2 * 43000 beta + 2 * 22700 gamma, sedimentation velocity, SDS-PAGE, amino acid analysis
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(alphabetagamma)2, 1 * 59900, alpha-subunit, + 1 * 45200, beta-subunit, 1 * 19300, gamma-subunit, SDS-PAGE
hexamer
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(alphabetagamma)2, 1 * 59900, alpha-subunit, + 1 * 45200, beta-subunit, 1 * 19300, gamma-subunit, SDS-PAGE
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hexamer
Methylosinus sporium ATCC 35069
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(alphabetagamma)2, 1 * 59900, alpha-subunit, + 1 * 45200, beta-subunit, 1 * 19300, gamma-subunit, SDS-PAGE
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hexamer
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2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
hexamer
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2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
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A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
1 * 245000, alpha-subunitMMOH, + 1 * 37000, beta-subunit MMOR, + 1 * 15000, gamma-subunit MMOB
trimer
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
soluble methane monooxygenase (sMMO) is a multicomponent metalloenzyme, all three sMMO protein components are: hydroxylase (MMOH), reductase (MMOR), and regulatory protein (MMOB), (alphabetagamma)2, 1 * 245000, hydroxylase (sMMOH), + 1 * 38000, flavin adenine dinucleotide (FAD) and 2Fe-2S cluster-containing reductase (MMOR) + 1 * 1000 cofactorless regulatory component (MMOB)
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see under molecular weight for the size of the protein components
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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see under molecular weight for the size of the protein components
additional information
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see under molecular weight for the size of the protein components
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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sMMO consists of 4 components: a hydroxylase, a reductase, a protein B and a protein D
additional information
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enzyme structure, the enzyme consists of a hydroxylase protein MMOH and a regulatory reductase protein MMOR, comparison of MMOH-MMOR-ferrdoxin and MMOH-MMOR, binding interactions, overview
additional information
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enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
additional information
enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
additional information
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structural architecture of sMMO, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview. MMOR consists of a NAD binding domain, an FAD-binding domain and a ferredoxin and plays a key role in the delivery of electrons within sMMO enzyme systems. The Fe2S2 domain appears to be the MMOH (methane monooxygenase hydroxylase) binding site
additional information
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enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
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additional information
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structural architecture of sMMO, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview. MMOR consists of a NAD binding domain, an FAD-binding domain and a ferredoxin and plays a key role in the delivery of electrons within sMMO enzyme systems. The Fe2S2 domain appears to be the MMOH (methane monooxygenase hydroxylase) binding site
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additional information
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enzyme structure, the enzyme consists of a hydroxylase protein MMOH and a regulatory reductase protein MMOR, comparison of MMOH-MMOR-ferrdoxin and MMOH-MMOR, binding interactions, overview
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additional information
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see under molecular weight for the size of the protein components
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additional information
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enzyme system consists of 3 protein components A, B, C
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additional information
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sMMO consists of 4 components: a hydroxylase, a reductase, a protein B and a protein D
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additional information
Methylococcus capsulatus Bath.
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enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
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additional information
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sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase
additional information
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three-dimensional structure, the enzyme consists as three protein component system, the regulatory protein MMOB, containing Fe2S2 cluster and a FAD cofactor, binds to the active site-containing hydroxylase protein creating a pore sized for methane into the active site, the third component is termed B, the complex appears to cause quantum tunneling to dominate in CH bond cleavage reaction for methane, selectively increasing the rate for this substrate, overview
additional information
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see under molecular weight for the size of the protein components
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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the enzyme complex of sMMO is formed by different components, including hydroxylase (MMOH), regulatory (MMOB), and reductase (MMOR)
additional information
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the enzyme complex of sMMO is formed by different components, including hydroxylase (MMOH), regulatory (MMOB), and reductase (MMOR)
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additional information
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see under molecular weight for the size of the protein components
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additional information
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enzyme system consists of 3 protein components A, B, C
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additional information
Methylosinus sporium ATCC 35069
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the enzyme complex of sMMO is formed by different components, including hydroxylase (MMOH), regulatory (MMOB), and reductase (MMOR)
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additional information
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see under molecular weight for the size of the protein components
additional information
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see under molecular weight for the size of the protein components
additional information
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see under molecular weight for the size of the protein components
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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3 components: 1 soluble CO-binding cytochrome c, 1 copper-containing protein, and 1 small protein, SDS-PAGE
additional information
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interaction of the soluble methane monooxygenase regulatory component, MMOB, and the active site-bearing hydroxylase component, MMOH, spin labeling with 4-maleimido-2,2,6,6-tetramethyl-1-piperidinyloxy, high affinity of labeled MMOB for the oxidized MMOH decreases substantially with increasing pH and increasing ionic strength but is nearly unaffected by addition of nonionic detergents, the MMOB-MMOH complex is stabilized by electrostatic interactions, overview
additional information
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the enzyme mainly exists of alpha-helical regions, circular dichroism measurement
additional information
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
the sMMO enzyme consists of three protein components: a 245 kDa (alphabetagamma)2 hydroxylase (MMOH), a 37 kDa FAD and Fe2S2 cluster-containing reductase (MMOR), and a 15 kDa regulatory protein (MMOB). The active site is buried deep within sMMOH and contains an oxygen-bridged dinuclear FeIII cluster in which the irons are bridged by two hydroxo moieties and a carboxylate from Glu144. After reduction, the diiron cluster functions to activate O2 and insert an oxygen atom into a highly stable (105 kcal/mol bond dissociation energy) C-H bond of methane. Although chemically reduced sMMOH can carry out the oxygenation chemistry alone, the reaction only proceeds at a physiologically relevant rate when sMMOH is complexed with MMOB. Reduction of the diiron cluster causes a shift in the position of Glu243, a monodentate ligand to Fe2 in the diferric cluster. In the shifted position, Glu243 bridges Fe1 and Fe2 via one of its carboxylate oxygens, thereby directly displacing one of the bridging solvents. The second bridging solvent bond is weakened, which presumably allows facile displacement by O2 to begin the oxygen activation process
additional information
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the enzyme mainly exists of alpha-helical regions, circular dichroism measurement
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additional information
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protein comprises a [2Fe-2S] ferredoxin domain, NAD(P)H-dependent FAD-containing reductase domain, FCD domain, and cytochrome P450 domain, in that order from the N terminus
additional information
Paraburkholderia terrae KU-64
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protein comprises a [2Fe-2S] ferredoxin domain, NAD(P)H-dependent FAD-containing reductase domain, FCD domain, and cytochrome P450 domain, in that order from the N terminus
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