BRENDA - Enzyme Database show
show all sequences of 1.3.5.4

Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum

Shimizu, H.; Osanai, A.; Sakamoto, K.; Inaoka, D.K.; Shiba, T.; Harada, S.; Kita, K.; J. Biochem. 151, 589-592 (2012)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
purified native enzyme by dialysis method using a reservoir solution containing 15% w/v PEG 3350, 100 mM Tris-HCl, pH 8.4, 200 mM NaCl, 1 mM sodium malonate or fumarate, 0.06% w/v n-dodecyl ethylene glycol monoether C12E8, and 0.04% w/v n-dodecyl-bet-D-maltoside, 2-3 days, X-ray diffraction structure determination and analysis at 2.81-2.91 A resolution, molecular replacement
Ascaris suum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Ascaris suum
5739
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
of the three iron-sulfur centres bound to subunit Ip, [2Fe-2S] is coordinated by four cysteine residues,B89, B94, B97 and B109, and located in the N-terminal domain, whereas [4Fe-4S] and [3Fe-4S] that are coordinated by four, B182, B185, B188, and B249, and three, B192, B239 and B245, cysteine residues, respectively, are bound to the C-terminal domain. These iron-sulfur centres are also surrounded with highly conserved hydrophobic amino acid residues
Ascaris suum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
succinate + rhodoquinone
Ascaris suum
-
fumarate + rhodoquinol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ascaris suum
P92507
-
-
Purification (Commentary)
Commentary
Organism
native enzyme from muscle mitochondria by anion exchange chromatography
Ascaris suum
Source Tissue
Source Tissue
Commentary
Organism
Textmining
muscle
-
Ascaris suum
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
succinate + rhodoquinone
-
725316
Ascaris suum
fumarate + rhodoquinol
-
-
-
?
succinate + rhodoquinone
rhodoquinone binding site, overview
725316
Ascaris suum
fumarate + rhodoquinol
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
the enzyme structure comprises four subunits and five co-factors, subunit structure comparisons, overview
Ascaris suum
tetramer
QFR is composed of Fp, Ip, CybL and CybS subunits
Ascaris suum
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
the FAD prosthetic group is held in the FAD binding domain by a covalent bond to His A79 and by hydrogen bonds with highly conserved residues, overview
Ascaris suum
heme
-
Ascaris suum
additional information
the enzyme structure comprises four subunits and five co-factors, cofactor structure comparisons, overview
Ascaris suum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
the FAD prosthetic group is held in the FAD binding domain by a covalent bond to His A79 and by hydrogen bonds with highly conserved residues, overview
Ascaris suum
heme
-
Ascaris suum
additional information
the enzyme structure comprises four subunits and five co-factors, cofactor structure comparisons, overview
Ascaris suum
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified native enzyme by dialysis method using a reservoir solution containing 15% w/v PEG 3350, 100 mM Tris-HCl, pH 8.4, 200 mM NaCl, 1 mM sodium malonate or fumarate, 0.06% w/v n-dodecyl ethylene glycol monoether C12E8, and 0.04% w/v n-dodecyl-bet-D-maltoside, 2-3 days, X-ray diffraction structure determination and analysis at 2.81-2.91 A resolution, molecular replacement
Ascaris suum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Ascaris suum
5739
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
of the three iron-sulfur centres bound to subunit Ip, [2Fe-2S] is coordinated by four cysteine residues,B89, B94, B97 and B109, and located in the N-terminal domain, whereas [4Fe-4S] and [3Fe-4S] that are coordinated by four, B182, B185, B188, and B249, and three, B192, B239 and B245, cysteine residues, respectively, are bound to the C-terminal domain. These iron-sulfur centres are also surrounded with highly conserved hydrophobic amino acid residues
Ascaris suum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
succinate + rhodoquinone
Ascaris suum
-
fumarate + rhodoquinol
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme from muscle mitochondria by anion exchange chromatography
Ascaris suum
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
muscle
-
Ascaris suum
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
succinate + rhodoquinone
-
725316
Ascaris suum
fumarate + rhodoquinol
-
-
-
?
succinate + rhodoquinone
rhodoquinone binding site, overview
725316
Ascaris suum
fumarate + rhodoquinol
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
the enzyme structure comprises four subunits and five co-factors, subunit structure comparisons, overview
Ascaris suum
tetramer
QFR is composed of Fp, Ip, CybL and CybS subunits
Ascaris suum
General Information
General Information
Commentary
Organism
additional information
enzyme structure-function relationship, overview
Ascaris suum
physiological function
the enzyme is part of the complex II, which in the anaerobic respiratory chain of the parasitic nematode Ascaris suum, couples the reduction of fumarate to the oxidation of rhodoquinol. Critical role of the low redox potential of rhodoquinol in the fumarate reduction of Ascaris suum complex II
Ascaris suum
General Information (protein specific)
General Information
Commentary
Organism
additional information
enzyme structure-function relationship, overview
Ascaris suum
physiological function
the enzyme is part of the complex II, which in the anaerobic respiratory chain of the parasitic nematode Ascaris suum, couples the reduction of fumarate to the oxidation of rhodoquinol. Critical role of the low redox potential of rhodoquinol in the fumarate reduction of Ascaris suum complex II
Ascaris suum
Other publictions for EC 1.3.5.4
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)
743255
Kassem
The impairment of methylmenaq ...
Campylobacter jejuni subsp. jejuni
MicrobiologyOpen
3
168-181
2014
-
-
-
-
-
-
-
-
-
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1
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-
-
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-
-
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-
-
1
1
-
-
-
742846
Singh
Plasticity of the quinone-bin ...
Escherichia coli
J. Biol. Chem.
288
24293-24301
2013
-
-
1
1
9
-
-
15
-
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-
1
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-
3
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33
-
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2
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1
2
1
9
-
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15
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-
3
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33
-
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-
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-
743059
Nasiri
Design, synthesis, and biolog ...
Wolinella succinogenes, Wolinella succinogenes DSM 1740
J. Med. Chem.
56
9530-9541
2013
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-
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2
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2
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4
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4
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4
2
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4
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-
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-
724561
Herzog
Hydrogen-bonded networks along ...
Campylobacter jejuni, Helicobacter pylori, Wolinella succinogenes
Biophys. J.
103
1305-1314
2012
-
-
-
-
3
-
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-
3
-
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-
3
-
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2
3
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6
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6
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3
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3
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2
3
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3
3
-
-
-
725316
Shimizu
Crystal structure of mitochond ...
Ascaris suum
J. Biochem.
151
589-592
2012
-
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-
1
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1
1
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1
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1
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1
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1
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2
2
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3
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3
1
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1
1
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1
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1
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1
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2
2
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2
2
-
-
-
700278
Juhnke
Production, characterization a ...
Campylobacter jejuni, Wolinella succinogenes
Mol. Microbiol.
71
1088-1101
2009
-
-
-
-
1
-
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2
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1
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5
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1
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1
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1
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1
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2
-
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1
1
1
1
-
-
707545
Xin
Purification, characterization ...
Chloroflexus aurantiacus
Biochim. Biophys. Acta
1787
86-96
2009
-
-
-
1
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1
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1
1
4
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1
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1
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1
1
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1
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1
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1
1
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707949
Garcia
The succinate:menaquinone redu ...
Bacillus cereus
Can. J. Microbiol.
54
456-466
2008
-
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-
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2
2
1
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3
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1
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1
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2
1
1
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1
1
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2
1
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2
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2
1
2
1
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1
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2
1
1
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1
1
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674532
Maklashina
Fumarate reductase and succina ...
Escherichia coli
J. Biol. Chem.
281
11357-11365
2006
-
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-
1
3
-
2
5
-
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1
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1
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2
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6
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6
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1
3
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2
6
5
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1
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-
2
-
-
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-
6
-
-
-
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5
5
674634
Maklashina
Differences in protonation of ...
Escherichia coli
J. Biol. Chem.
281
26655-26664
2006
-
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4
-
1
2
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1
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3
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7
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2
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4
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1
2
2
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3
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7
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707470
Madej
Experimental evidence for prot ...
Bacillus licheniformis
Biochemistry
45
15049-15055
2006
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1
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5
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1
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3
1
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1
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1
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3
1
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671694
Fernandes
Quinone reduction by Rhodother ...
Rhodothermus marinus
Biochem. Biophys. Res. Commun.
330
565-570
2005
-
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1
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1
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1
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654820
Cecchini
Succinate dehydrogenase and fu ...
Escherichia coli
Biochim. Biophys. Acta
1553
140-157
2002
-
-
1
1
1
-
2
3
1
1
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2
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1
1
1
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3
1
1
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1
4
-
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1
1
1
1
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-
2
4
3
1
1
-
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-
-
1
1
1
-
-
3
1
1
-
-
1
1
1
1
-
-
708975
Iverson
Crystallographic studies of th ...
Escherichia coli
J. Biol. Chem.
277
16124-16130
2002
-
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1
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2
-
1
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1
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708368
Schnorpfeil
Generation of a proton potenti ...
Bacillus subtilis
Eur. J. Biochem.
268
3069-3074
2001
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1
1
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391149
Lancaster
Succinate:quinone oxidoreducta ...
Escherichia coli, Wolinella succinogenes
Biochim. Biophys. Acta
1459
422-431
2000
-
-
-
1
-
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1
1
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1
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2
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2
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3
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3
1
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1
1
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1
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2
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2
2
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708909
Maklashina
Anaerobic expression of Escher ...
Escherichia coli
J. Bacteriol.
180
5989-5996
1998
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1
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1
1
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708966
Schroder
Identification of active site ...
Escherichia coli
J. Biol. Chem.
266
13572-13579
1991
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-
-
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4
-
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4
-
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2
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1
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1
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4
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2
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391090
Körtner
Wolinella succinogenes fumarat ...
Wolinella succinogenes
Mol. Microbiol.
4
855-860
1990
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1
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1
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1
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1
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1
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1
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2
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391089
Lauterbach
Cloning and expression of the ...
Wolinella succinogenes
Eur. J. Biochem.
166
447-452
1987
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1
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1
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1
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1
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2
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2
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391106
Weiner
A mutant of Escherichia coli f ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
83
2056-2060
1986
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4
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1
1
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391147
Gottfried
Reconstitution of a functional ...
Wolinella succinogenes
Methods Enzymol.
126
387-399
1986
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710440
Cecchini
Oxidation of reduced menaquino ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
83
8898-8902
1986
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1
1
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391094
Unden
-
Redox potentials and kinetic p ...
Wolinella succinogenes
Biochim. Biophys. Acta
767
460-469
1984
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391084
Unden
The function of the subunits o ...
Wolinella succinogenes
Eur. J. Biochem.
120
577-584
1981
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2
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1
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391092
Unden
Isolation and functional aspec ...
Wolinella succinogenes
Biochim. Biophys. Acta
591
275-288
1980
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6
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2
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391116
Kröger
The orientation of the substra ...
Wolinella succinogenes
Biochim. Biophys. Acta
589
118-136
1980
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707291
Van der Beek
Fumarate reduction in Proteus ...
Proteus mirabilis
Arch. Microbiol.
110
195-206
1976
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2
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2
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2
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708369
Kroeger
-
The function of menaquinone, c ...
Wolinella succinogenes
Eur. J. Biochem.
69
487-495
1976
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1
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