BRENDA - Enzyme Database show
show all sequences of 1.14.18.3

Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy

Lieberman, R.L.; Kondapalli, K.C.; Shrestha, D.B.; Hakemian, A.S.; Smith, S.M.; Telser, J.; Kuzelka, J.; Gupta, R.; Borovik, A.S.; Lippard, S.J.; Hoffman, B.M.; Rosenzweig, A.C.; Stemmler, T.L.; Inorg. Chem. 45, 8372-8381 (2006)

Data extracted from this reference:

Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Cu2+
the enzyme contains a mononuclear copper center and a dinuclear copper center, Cu-Cu interaction occurs in all redox forms of the enzyme, usage of mixed-valent dinuclear Cu model compounds, [tris{(N'-tert-butylureaylato)-N-ethyl}aminatocopper(II)]2BF4, and [N-tert-butylurealylato-{2-(dimethylamino)ethyl}aminatocopper(II)]2BF4, which are blue, and purple samples of [Cu2(m-xylylenediaminebis(Kemps triacid imide))(my-OTf)(THF)2], and [Cu2(m-xylylenediaminebis(Kemps triacid imide))(my-O2CCF3)(THF)2], EXAFS and Fourier transformation analysis, detailed interaction analysis, overview
Methylococcus capsulatus
additional information
analysis of the oxidation states and coordination environments of the pMMO metal centers, overview
Methylococcus capsulatus
Zn2+
the enzyme contains a nonphysiological mononuclear zinc center
Methylococcus capsulatus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
methane + NADH + O2
Methylococcus capsulatus
-
methanol + NAD+ + H2O
-
-
?
methane + NADH + O2
Methylococcus capsulatus Bath
-
methanol + NAD+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methylococcus capsulatus
-
-
-
Methylococcus capsulatus Bath
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
methane + NADH + O2
-
674005
Methylococcus capsulatus
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + O2
-
674005
Methylococcus capsulatus Bath
methanol + NAD+ + H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Methylococcus capsulatus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Methylococcus capsulatus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Cu2+
the enzyme contains a mononuclear copper center and a dinuclear copper center, Cu-Cu interaction occurs in all redox forms of the enzyme, usage of mixed-valent dinuclear Cu model compounds, [tris{(N'-tert-butylureaylato)-N-ethyl}aminatocopper(II)]2BF4, and [N-tert-butylurealylato-{2-(dimethylamino)ethyl}aminatocopper(II)]2BF4, which are blue, and purple samples of [Cu2(m-xylylenediaminebis(Kemps triacid imide))(my-OTf)(THF)2], and [Cu2(m-xylylenediaminebis(Kemps triacid imide))(my-O2CCF3)(THF)2], EXAFS and Fourier transformation analysis, detailed interaction analysis, overview
Methylococcus capsulatus
additional information
analysis of the oxidation states and coordination environments of the pMMO metal centers, overview
Methylococcus capsulatus
Zn2+
the enzyme contains a nonphysiological mononuclear zinc center
Methylococcus capsulatus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
methane + NADH + O2
Methylococcus capsulatus
-
methanol + NAD+ + H2O
-
-
?
methane + NADH + O2
Methylococcus capsulatus Bath
-
methanol + NAD+ + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
methane + NADH + O2
-
674005
Methylococcus capsulatus
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + O2
-
674005
Methylococcus capsulatus Bath
methanol + NAD+ + H2O
-
-
-
?
Other publictions for EC 1.14.18.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744037
Cao
Quantum refinement does not s ...
Methylococcus capsulatus, Methylococcus capsulatus Bath
Angew. Chem. Int. Ed. Engl.
57
162 -166
2018
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1
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744688
Wang
Alkane oxidation methane mono ...
Methylococcus capsulatus, Methylococcus capsulatus Bath
Chem. Rev.
117
8574-8621
2017
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13
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744923
Wang
An improved protocol with a h ...
uncultured Alphaproteobacteria bacterium, uncultured gamma proteobacterium
FEMS Microbiol. Ecol.
93
fiw244
2017
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4
2
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745389
Ross
A tale of two methane monooxy ...
Methylococcus capsulatus, Methylococcus capsulatus Bath., Methylococcus capsulatus Bath, Methylocystis sp., Methylocystis sp. M, Methylocystis sp. Rockwell, Methylosinus trichosporium
J. Biol. Inorg. Chem.
22
307-319
2017
1
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1
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2
6
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3
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22
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2
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9
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2
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1
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2
1
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2
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3
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9
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6
6
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-
745453
Zhang
Coupled effects of methane mo ...
Methylosinus trichosporium
J. Environ. Sci.
52
49-57
2017
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1
1
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745536
Nguyen
A novel methanotroph in the g ...
Methylomonas sp., Methylomonas sp. EMGL16-1
J. Microbiol.
55
775-782
2017
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746420
Zhang
-
Low-temperature biological ac ...
Methylococcus capsulatus, Methylococcus capsulatus Bath, Methylocystis sp., Methylocystis sp. Rockwell, Methylosinus trichosporium
Rev. Environ. Sci. Biotechnol.
16
611-623
2017
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1
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3
5
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2
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18
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5
1
3
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2
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3
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1
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3
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3
5
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2
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5
1
3
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2
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2
2
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745067
Itoyama
Possible peroxo state of the ...
Methylococcus capsulatus, Methylococcus capsulatus Bath
Inorg. Chem.
55
2771-2775
2016
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1
1
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13
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1
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745730
Larsen
Transcriptomic profiling of M ...
Methylococcus capsulatus, Methylococcus capsulatus Bath., Methylococcus capsulatus Bath
MicrobiologyOpen
5
254-267
2016
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1
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5
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16
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1
2
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745857
Blanchette
Printable enzyme-embedded mat ...
Methylococcus capsulatus, Methylococcus capsulatus Bath
Nat. Commun.
7
11900
2016
-
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1
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1
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4
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744098
Kalidass
Competition between metals fo ...
Methylosinus trichosporium
Appl. Environ. Microbiol.
81
1024-1031
2015
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1
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1
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744405
Pham
Inactivation of the particula ...
Methylococcus capsulatus, Methylococcus capsulatus Bath
Biochim. Biophys. Acta
1854
1842-1852
2015
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4
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1
1
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13
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2
2
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1
1
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744325
Culpepper
Structure and protein-protein ...
Methylococcus capsulatus, Methylococcus capsulatus Bath
Biochemistry
53
6211-6219
2014
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1
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15
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1
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1
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745154
Culpepper
Identification of the valence ...
Methylococcus capsulatus, Methylococcus capsulatus Bath
J. Am. Chem. Soc.
136
11767-11775
2014
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4
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1
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14
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745305
Sirajuddin
Effects of zinc on particulat ...
Methylococcus capsulatus, Methylococcus capsulatus Bath, Methylocystis sp., Methylocystis sp. Rockwell
J. Biol. Chem.
289
21782-21794
2014
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17
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3
2
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1
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745721
Liew
Mutagenesis of the hydrocarbo ...
Methylococcus capsulatus, Methylococcus capsulatus Bath, Methylocystis sp., Methylosinus trichosporium
Microbiology
160
1267-1277
2014
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16
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6
6
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727340
Culpepper
Architecture and active site o ...
Methylococcus capsulatus, Methylocystis sp., Methylosinus trichosporium
Crit. Rev. Biochem. Mol. Biol.
47
483-492
2012
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3
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727434
Erikstad
Differential expression of par ...
Methylacidiphilum kamchatkense, Methylacidiphilum kamchatkense Kam1
Extremophiles
16
405-409
2012
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727552
Wu
Co-localization of particulate ...
Candidatus Methylomirabilis oxyfera
FEMS Microbiol. Lett.
334
49-56
2012
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727681
Culpepper
Evidence for oxygen binding at ...
Methylococcus capsulatus
J. Am. Chem. Soc.
134
7640-7643
2012
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3
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1
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728079
Chen
Bacteriohemerythrin bolsters t ...
Methylococcus capsulatus
J. Inorg. Biochem.
111
10-17
2012
1
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1
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3
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1
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1
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716108
Chan
Overexpression and purificatio ...
Methylococcus capsulatus, Methylococcus capsulatus ATCC 33009
Methods Enzymol.
495
177-193
2011
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1
1
11
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In situ measurement of methane ...
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Miyaji
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Hydrogen peroxide as an effect ...
Methylosinus trichosporium OB3b
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2009
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Chan
Controlled oxidation of hydroc ...
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686085
Ng
Probing the hydrophobic pocket ...
Methylococcus capsulatus
ChemBioChem
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Baani
Two isozymes of particulate me ...
Methylocystis sp., Methylocystis sp. Sc2
Proc. Natl. Acad. Sci. USA
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Tumanova
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The binuclear iron site of mem ...
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702170
Rosenzweig
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Purification and properties of ...
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Anthony
A tribute to Howard Dalton and ...
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684112
Balasubramanian
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685113
Yu
The C-terminal aqueous-exposed ...
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Biochemistry
46
13762-13774
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Nakamura
Soluble and particulate methan ...
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687284
Martinho
Moessbauer studies of the memb ...
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690012
Hayashi
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Molecular diversity of the gen ...
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Lee
Mixed pollutant degradation by ...
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672301
Vasilev
Optimization of solubilization ...
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Gou
Functional expression of the p ...
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Lieberman
Characterization of the partic ...
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671965
Kitmitto
Characterization and structura ...
Methylococcus capsulatus, Methylococcus capsulatus Bath
Biochemistry
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675831
Choi
Effect of methanobactin on the ...
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Microbiology
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Basu
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The membrane-associated methan ...
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Lieberman
Purified particulate methane m ...
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2
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Xin
Particulate methane monooxygen ...
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438942
Murrell
Molecular biology and regulati ...
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3
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6
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13
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46
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13
3
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6
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13
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13
3
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3
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3
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Nguyen
The particulate methane monoox ...
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4
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1
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1
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Zahn
Membrane-associated methane mo ...
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2
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7
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2
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1
8
2
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713934
Shiemke
Detergent solubilization of me ...
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2
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14
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438927
Cornish
-
Succinate as an in vitro elect ...
Methylosinus trichosporium
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1985
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1
1
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438940
Tonge
Properties and partial purific ...
Methylosinus trichosporium
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58
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1975
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