BRENDA - Enzyme Database
show all sequences of 1.3.5.4

Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site

Iverson, T.M.; Luna-Chavez, C.; Croal, L.R.; Cecchini, G.; Rees, D.C.; J. Biol. Chem. 277, 16124-16130 (2002)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystal structure of QFR to 3.3 A resolution. Enzyme contains two quinone species, presumably menaquinol, bound to the transmembrane-spanning region. The binding sites for the two quinone molecules are termed QP and QD, indicating their positions proximal, QP, or distal, QD, to the site of fumarate reduction in the hydrophilic flavoprotein and iron-sulfur protein subunits. Co-crystallization studies of the Escherichia coli QFR with the quinol-binding site inhibitors 2-heptyl-4-hydroxyquinoline-N-oxide and 2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol establish that both inhibitors block the binding of MQH2 at the QP site. In the structures with the inhibitor bound at QP, no density is observed at QD. The conserved acidic residue, Glu29 in subunit FrdC, in the Escherichia coli enzyme may act as a proton shuttle from the quinol during enzyme turnover
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-heptyl-4-hydroxyquinoline N-oxide
inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies
Escherichia coli
2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol
inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies
Escherichia coli
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Escherichia coli
16020
-
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
P00363
-
-
Synonyms
Synonyms
Commentary
Organism
QFR
-
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure of QFR to 3.3 A resolution. Enzyme contains two quinone species, presumably menaquinol, bound to the transmembrane-spanning region. The binding sites for the two quinone molecules are termed QP and QD, indicating their positions proximal, QP, or distal, QD, to the site of fumarate reduction in the hydrophilic flavoprotein and iron-sulfur protein subunits. Co-crystallization studies of the Escherichia coli QFR with the quinol-binding site inhibitors 2-heptyl-4-hydroxyquinoline-N-oxide and 2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol establish that both inhibitors block the binding of MQH2 at the QP site. In the structures with the inhibitor bound at QP, no density is observed at QD. The conserved acidic residue, Glu29 in subunit FrdC, in the Escherichia coli enzyme may act as a proton shuttle from the quinol during enzyme turnover
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-heptyl-4-hydroxyquinoline N-oxide
inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies
Escherichia coli
2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol
inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Escherichia coli
16020
-
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
Synonyms
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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742846
Singh
Plasticity of the quinone-bin ...
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Shimizu
Crystal structure of mitochond ...
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2012
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Purification, characterization ...
Chloroflexus aurantiacus
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The succinate:menaquinone redu ...
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Maklashina
Fumarate reductase and succina ...
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674634
Maklashina
Differences in protonation of ...
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Madej
Experimental evidence for prot ...
Bacillus licheniformis
Biochemistry
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671694
Fernandes
Quinone reduction by Rhodother ...
Rhodothermus marinus
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2005
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654820
Cecchini
Succinate dehydrogenase and fu ...
Escherichia coli
Biochim. Biophys. Acta
1553
140-157
2002
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708975
Iverson
Crystallographic studies of th ...
Escherichia coli
J. Biol. Chem.
277
16124-16130
2002
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Schnorpfeil
Generation of a proton potenti ...
Bacillus subtilis
Eur. J. Biochem.
268
3069-3074
2001
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Lancaster
Succinate:quinone oxidoreducta ...
Escherichia coli, Wolinella succinogenes
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2000
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Maklashina
Anaerobic expression of Escher ...
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1998
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Wolinella succinogenes fumarat ...
Wolinella succinogenes
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Wolinella succinogenes
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Weiner
A mutant of Escherichia coli f ...
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83
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1986
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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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391094
Unden
-
Redox potentials and kinetic p ...
Wolinella succinogenes
Biochim. Biophys. Acta
767
460-469
1984
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1
1
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-
2
-
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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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-
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-
-
-
-
-
-
-
3
2
-
1
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-
1
-
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4
1
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-
1
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-
-
2
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2
-
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3
2
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1
-
-
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4
1
-
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-
1
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-
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391092
Unden
Isolation and functional aspec ...
Wolinella succinogenes
Biochim. Biophys. Acta
591
275-288
1980
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-
-
-
-
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-
1
1
1
6
-
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1
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1
-
-
-
1
-
2
2
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-
-
-
-
-
-
-
3
-
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-
-
-
3
-
-
-
-
-
-
1
1
1
6
-
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-
1
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-
1
-
2
2
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-
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391116
Kröger
The orientation of the substra ...
Wolinella succinogenes
Biochim. Biophys. Acta
589
118-136
1980
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-
-
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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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1
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-
707291
Van der Beek
Fumarate reduction in Proteus ...
Proteus mirabilis
Arch. Microbiol.
110
195-206
1976
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-
-
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-
-
2
-
1
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1
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2
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1
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-
2
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-
2
-
-
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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2
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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1
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2
1
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1
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1
1
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