BRENDA - Enzyme Database show
show all sequences of 1.3.5.4

Hydrogen-bonded networks along and bifurcation of the E-pathway in quinol:fumarate reductase

Herzog, E.; Gu, W.; Juhnke, H.D.; Haas, A.H.; Maentele, W.; Simon, J.; Helms, V.; Lancaster, C.R.; Biophys. J. 103, 1305-1314 (2012)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
E180Q
site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
Wolinella succinogenes
E66Q
site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
Wolinella succinogenes
H44E
site-diirected mutagenesis, although the H44E variant enzyme retains both heme groups, it is unable to catalyze quinol oxidation, the mutant catalyzes the electron transfer from succinate to methylene blue, with reduced activity compared to the wild-type enzyme but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
Wolinella succinogenes
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
bound
Campylobacter jejuni
16020
-
membrane
bound
Helicobacter pylori
16020
-
membrane
bound
Wolinella succinogenes
16020
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Campylobacter jejuni
-
-
-
Helicobacter pylori
-
-
-
Wolinella succinogenes
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-dimethyl-1,4-naphthoquinol + fumarate
-
724561
Wolinella succinogenes
?
-
-
-
?
succinate + methylene blue
-
724561
Wolinella succinogenes
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
oligomer
homodimeric complex of heterotrimers of A, B, and C subunits
Campylobacter jejuni
oligomer
homodimeric complex of heterotrimers of A, B, and C subunits
Helicobacter pylori
oligomer
homodimeric complex of heterotrimers of A, B, and C subunits
Wolinella succinogenes
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Campylobacter jejuni
FAD
-
Helicobacter pylori
FAD
-
Wolinella succinogenes
heme
a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B
Campylobacter jejuni
heme
a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B
Helicobacter pylori
heme
a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B
Wolinella succinogenes
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Campylobacter jejuni
FAD
-
Helicobacter pylori
FAD
-
Wolinella succinogenes
heme
a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B
Campylobacter jejuni
heme
a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B
Helicobacter pylori
heme
a diheme-containing enzyme, each heterotrimer contains two heme b groups bound by the transmembrane subunit C, which are termed the proximal heme, bP, and the distal heme, bD, according to the relative proximity to the hydrophilic subunits A and B
Wolinella succinogenes
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E180Q
site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
Wolinella succinogenes
E66Q
site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
Wolinella succinogenes
H44E
site-diirected mutagenesis, although the H44E variant enzyme retains both heme groups, it is unable to catalyze quinol oxidation, the mutant catalyzes the electron transfer from succinate to methylene blue, with reduced activity compared to the wild-type enzyme but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
Wolinella succinogenes
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
bound
Campylobacter jejuni
16020
-
membrane
bound
Helicobacter pylori
16020
-
membrane
bound
Wolinella succinogenes
16020
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-dimethyl-1,4-naphthoquinol + fumarate
-
724561
Wolinella succinogenes
?
-
-
-
?
succinate + methylene blue
-
724561
Wolinella succinogenes
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
oligomer
homodimeric complex of heterotrimers of A, B, and C subunits
Campylobacter jejuni
oligomer
homodimeric complex of heterotrimers of A, B, and C subunits
Helicobacter pylori
oligomer
homodimeric complex of heterotrimers of A, B, and C subunits
Wolinella succinogenes
General Information
General Information
Commentary
Organism
additional information
the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview
Campylobacter jejuni
additional information
the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview
Helicobacter pylori
additional information
the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview
Wolinella succinogenes
General Information (protein specific)
General Information
Commentary
Organism
additional information
the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview
Campylobacter jejuni
additional information
the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview
Helicobacter pylori
additional information
the E-pathway of transmembrane proton transfer is essential for catalysis by the diheme-containing quinol:fumarate reductase, molecular dynamics simulations, overview. The redox state of heme groups has a crucial effect on the connectivity patterns of mobile internal water molecules that can transiently support proton transfer from the bD-C-propionate to Glu-C180. The short H-bonding paths formed in the reduced states can lead to high proton conduction rates. The bD-C-propionate group is the branching point connecting proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme bD ligand His-C44, essential functional role of His-C44, hydrogen-bonded networks between the bD-C-propionate and Glu180, overview
Wolinella succinogenes
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
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
742846
Singh
Plasticity of the quinone-bin ...
Escherichia coli
J. Biol. Chem.
288
24293-24301
2013
-
-
1
1
9
-
-
15
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
33
-
-
-
2
-
-
-
-
-
1
2
1
9
-
-
-
-
15
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
33
-
-
-
-
-
-
-
-
-
-
743059
Nasiri
Design, synthesis, and biolog ...
Wolinella succinogenes, Wolinella succinogenes DSM 1740
J. Med. Chem.
56
9530-9541
2013
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
4
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
724561
Herzog
Hydrogen-bonded networks along ...
Campylobacter jejuni, Helicobacter pylori, Wolinella succinogenes
Biophys. J.
103
1305-1314
2012
-
-
-
-
3
-
-
-
3
-
-
-
-
3
-
-
-
-
-
-
-
-
2
3
-
-
-
-
-
-
-
6
-
-
-
-
-
-
6
-
3
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
2
3
-
-
-
-
-
-
-
-
-
3
3
-
-
-
725316
Shimizu
Crystal structure of mitochond ...
Ascaris suum
J. Biochem.
151
589-592
2012
-
-
-
1
-
-
-
-
1
1
-
1
-
1
-
-
1
-
-
1
-
-
2
2
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
1
-
-
-
-
-
-
1
1
-
1
-
-
-
1
-
1
-
-
2
2
-
-
-
-
-
-
-
-
-
2
2
-
-
-
700278
Juhnke
Production, characterization a ...
Campylobacter jejuni, Wolinella succinogenes
Mol. Microbiol.
71
1088-1101
2009
-
-
-
-
1
-
-
-
2
-
-
1
-
5
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
2
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
707545
Xin
Purification, characterization ...
Chloroflexus aurantiacus
Biochim. Biophys. Acta
1787
86-96
2009
-
-
-
1
-
-
1
-
1
1
4
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
1
-
-
-
1
-
-
1
1
4
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
707949
Garcia
The succinate:menaquinone redu ...
Bacillus cereus
Can. J. Microbiol.
54
456-466
2008
-
-
-
-
-
-
2
2
1
-
-
-
-
3
-
-
-
1
-
-
1
-
2
1
1
-
-
1
1
-
-
2
1
-
-
-
-
-
2
-
-
-
-
2
1
2
1
-
-
-
-
-
-
-
-
-
1
-
2
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
674532
Maklashina
Fumarate reductase and succina ...
Escherichia coli
J. Biol. Chem.
281
11357-11365
2006
-
-
-
1
3
-
2
5
-
-
-
-
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
6
-
-
-
-
6
-
-
-
-
-
-
1
3
-
-
2
6
5
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
5
5
674634
Maklashina
Differences in protonation of ...
Escherichia coli
J. Biol. Chem.
281
26655-26664
2006
-
-
-
-
4
-
1
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
7
-
-
-
-
2
-
-
-
-
-
-
-
4
-
-
1
2
2
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
707470
Madej
Experimental evidence for prot ...
Bacillus licheniformis
Biochemistry
45
15049-15055
2006
-
-
-
-
-
-
-
-
1
-
-
-
-
5
-
-
1
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671694
Fernandes
Quinone reduction by Rhodother ...
Rhodothermus marinus
Biochem. Biophys. Res. Commun.
330
565-570
2005
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
654820
Cecchini
Succinate dehydrogenase and fu ...
Escherichia coli
Biochim. Biophys. Acta
1553
140-157
2002
-
-
1
1
1
-
2
3
1
1
-
-
-
2
-
-
-
-
-
-
-
-
1
1
1
-
-
3
1
1
-
1
4
-
-
-
-
1
1
1
1
-
-
2
4
3
1
1
-
-
-
-
-
-
-
-
-
-
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
-
-
-
1
-
-
2
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
708368
Schnorpfeil
Generation of a proton potenti ...
Bacillus subtilis
Eur. J. Biochem.
268
3069-3074
2001
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
391149
Lancaster
Succinate:quinone oxidoreducta ...
Escherichia coli, Wolinella succinogenes
Biochim. Biophys. Acta
1459
422-431
2000
-
-
-
1
-
-
-
-
1
1
-
1
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
1
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
708909
Maklashina
Anaerobic expression of Escher ...
Escherichia coli
J. Bacteriol.
180
5989-5996
1998
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
708966
Schroder
Identification of active site ...
Escherichia coli
J. Biol. Chem.
266
13572-13579
1991
-
-
-
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391090
Körtner
Wolinella succinogenes fumarat ...
Wolinella succinogenes
Mol. Microbiol.
4
855-860
1990
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391089
Lauterbach
Cloning and expression of the ...
Wolinella succinogenes
Eur. J. Biochem.
166
447-452
1987
-
-
1
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391106
Weiner
A mutant of Escherichia coli f ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
83
2056-2060
1986
-
-
1
-
1
-
1
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391147
Gottfried
Reconstitution of a functional ...
Wolinella succinogenes
Methods Enzymol.
126
387-399
1986
-
-
-
-
-
-
-
-
-
1
4
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
4
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710440
Cecchini
Oxidation of reduced menaquino ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
83
8898-8902
1986
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
391094
Unden
-
Redox potentials and kinetic p ...
Wolinella succinogenes
Biochim. Biophys. Acta
767
460-469
1984
-
-
-
-
-
-
-
-
1
1
3
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
2
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
1
1
3
-
-
-
-
-
-
-
-
-
1
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
391084
Unden
The function of the subunits o ...
Wolinella succinogenes
Eur. J. Biochem.
120
577-584
1981
-
-
-
-
-
-
-
-
-
-
3
2
-
1
-
-
-
-
1
-
-
-
4
1
-
-
-
1
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
3
2
-
-
-
-
1
-
-
-
4
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
391092
Unden
Isolation and functional aspec ...
Wolinella succinogenes
Biochim. Biophys. Acta
591
275-288
1980
-
-
-
-
-
-
-
1
1
1
6
-
-
1
-
-
1
-
-
-
1
-
2
2
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
1
1
1
6
-
-
-
-
1
-
-
1
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391116
Kröger
The orientation of the substra ...
Wolinella succinogenes
Biochim. Biophys. Acta
589
118-136
1980
-
-
-
-
-
-
1
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
707291
Van der Beek
Fumarate reduction in Proteus ...
Proteus mirabilis
Arch. Microbiol.
110
195-206
1976
-
-
-
-
-
-
2
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
2
-
-
708369
Kroeger
-
The function of menaquinone, c ...
Wolinella succinogenes
Eur. J. Biochem.
69
487-495
1976
-
-
-
-
-
-
1
-
2
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
-
2
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-