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Information on EC 7.2.1.2 - ferredoxin-NAD+ oxidoreductase (Na+-transporting)
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7.2.1.2 ferredoxin-NAD+ oxidoreductase (Na+-transporting)IUBMB Comments
This iron-sulfur and flavin-containing electron transport complex, isolated from the bacterium Acetobacterium woodii, couples the energy from reduction of NAD+ by ferredoxin to pumping sodium ions out of the cell, generating a gradient across the cytoplasmic membrane.
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Word Map
- 7.2.1.2
-
acetogenic
- woodii
-
acetobacterium
-
wood-ljungdahl
-
chemiosmotic
-
endergonic
-
acetogenesis
-
syngas
-
fefe-hydrogenase
-
redox-driven
- na+-nqr
- ljungdahlii
-
electron-bifurcating
-
seafloor
-
genome-guided
-
aceticlastic
-
biocommodities
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
2
+
+
+
=
2
+
+
2
reduced ferredoxin [iron-sulfur] cluster
+
+
+
=
2
oxidized ferredoxin [iron-sulfur] cluster
+
+
Synonyms
rnf complex, rnf1 complex, ferredoxin:heterodisulfide oxidoreductase, na+-translocating ferredoxin:nad+ oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.18.1.8
-
-
formerly
-
ferredoxin:heterodisulfide oxidoreductase
ferredoxin:NAD+-oxidoreductase complex
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
-
Na+-translocating ferredoxin:NAD+-oxidoreductase
reduced ferredoxin:NAD+ oxidoreductase
Rnf
Rnf complex
rnfABCDEG
Rnf complex
Vibrio cholerae serotype O1 O395N-1
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] = 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ferredoxin:NAD+ oxidoreductase (Na+-transporting)
This iron-sulfur and flavin-containing electron transport complex, isolated from the bacterium Acetobacterium woodii, couples the energy from reduction of NAD+ by ferredoxin to pumping sodium ions out of the cell, generating a gradient across the cytoplasmic membrane.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 reduced ferredoxin + NAD+ + H+ + Na+in
2 oxidized ferredoxin + NADH + Na+out
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
-
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
2 reduced ferredoxin [iron-sulfur] cluster + methanophenazine + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + reduced methanophenazine + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
reduced flavodoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized flavodoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
-
-
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
-
electron transfer from reduced ferredoxin to NAD+ as acceptor drives the generation of a transmembrane ion gradient
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport. Low activity in absence of Na+
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
Acetobacterium woodii DSM 103
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
Acetobacterium woodii DSM 103
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport. Low activity in absence of Na+
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport. Low activity in absence of Na+
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
electron transfer from Fdred to NAD+ generates an Na+ potential
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
Na+ transport is directly linked to ferredoxin:NAD+ oxidoreductase activity and is electrogenic
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
Rnf's electron donation from NADH corresponds to inward flow of Na+
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
Vibrio cholerae serotype O1 O395N-1
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
Vibrio cholerae serotype O1 O395N-1
-
Rnf's electron donation from NADH corresponds to inward flow of Na+
-
-
?
reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
-
-
-
-
ir
reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
-
-
-
-
ir
reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
-
-
-
-
ir
reduced flavodoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized flavodoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
-
-
-
-
ir
reduced flavodoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized flavodoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
-
-
-
-
ir
reduced flavodoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized flavodoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
-
-
-
-
ir
additional information
?
-
the enzyme couples oxidation of reduced ferredoxin (generated by hydrogenase) with the reduction of NAD+. The Na+-translocating enzyme catalyzes electron transfer from ferredoxin to NAD+ coupled to electrogenic ion transport across the membrane
-
-
?
additional information
?
-
-
the enzyme couples oxidation of reduced ferredoxin (generated by hydrogenase) with the reduction of NAD+. The Na+-translocating enzyme catalyzes electron transfer from ferredoxin to NAD+ coupled to electrogenic ion transport across the membrane
-
-
?
additional information
?
-
the enzyme couples oxidation of reduced ferredoxin (generated by hydrogenase) with the reduction of NAD+. The Na+-translocating enzyme catalyzes electron transfer from ferredoxin to NAD+ coupled to electrogenic ion transport across the membrane
-
-
?
additional information
?
-
-
inside-out membrane vesicles of catalyze Na+ transport coupled to an electron transport catalyzed by theferredoxin:heterodisulfide oxidoreductase activity
-
-
?
additional information
?
-
-
K+ and Li+ do not stimulate oxidoreductase activity
-
-
-
additional information
?
-
-
presence of Na+ is absolutely required for activity. K+ may not substitute for Na+, Li+ substitues poorly
-
-
-
additional information
?
-
-
K+ and Li+ do not stimulate oxidoreductase activity
-
-
-
additional information
?
-
-
presence of Na+ is absolutely required for activity. K+ may not substitute for Na+, Li+ substitues poorly
-
-
-
additional information
?
-
-
the recombinant isolated RnfG produces a neutral semiquinone intermediate. The semiquinone species disappeared upon full reduction and is not observed in the denatured protein
-
-
?
additional information
?
-
Vibrio cholerae serotype O1 O395N-1
-
the recombinant isolated RnfG produces a neutral semiquinone intermediate. The semiquinone species disappeared upon full reduction and is not observed in the denatured protein
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
2 reduced ferredoxin [iron-sulfur] cluster + methanophenazine + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + reduced methanophenazine + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
-
electron transfer from reduced ferredoxin to NAD+ as acceptor drives the generation of a transmembrane ion gradient
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
Acetobacterium woodii DSM 103
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport
-
-
?
2 reduced ferredoxin iron-sulfur cluster + NAD+ + H+ + Na+/in
2 oxidized ferredoxin iron-sulfur cluster + NADH + Na+/out
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
Vibrio cholerae serotype O1 O395N-1
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
-
-
-
-
ir
reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
-
-
-
-
ir
reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+/[side 1]
oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+/[side 2]
-
-
-
-
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
Q8TSY0; Q8TSX9; Q8TSY4; Q8TSY3; Q8TSY1; Q8TSY2
subunit RnfB subunit shows a UV-visible spectrum typical of iron-sulfur proteins. EPR spectra of reduced RnfB featured a broad spectral shape characteristic of magnetically coupled 3Fe-4S and 4Fe-4S clusters. Ferredoxin specific to the aceticlastic pathway serves as an electron donor to RnfB
iron-sulfur centre
-
ironsulfur and flavin-containing electron transport complex
additional information
-
subunits RnfD and RnfG both contain the same motif, suggesting that they bind flavins in a similar way, mass spectroscopic analysis, overview. The flavins in RnfG and RnfD are localized in the periplasmic space
-
4Fe-4S-center
-
subunit RnfC contains 8.3 mol iron and 8.6 mol sulfur per mol of the subunit, consistent with the presence of two [4Fe-4S] centers. Isolated RnfC catalyzes NADH-dependent FMN reduction. Subunit RnfB contains 25 mol iron and 26 mol sulfur per mol, consistent with six [4Fe-4S] centers. The FeS centers in RnfB are reduced with reduced ferredoxin as reductant
Ferredoxin
-
RnfC contains two [4Fe-4S]-type ferredoxin-like domains
-
flavin
-
flavin covalently bound Thr187 in subunit RnfD. In RnfD, the flavin is bound, not to the SGAT sequence but to the final residues of a TMAT sequence, another variant of the flavin binding motif
flavin
-
noncovalently and covalently bound flavins in a polyferredoxin with four ferredoxin-like [4Fe-4S] centers in NfoB (RnfB)
FMN
-
covalently bound to Thr175 in subunit RnfG, the final threonine of the S(T)GAT sequence
FMN
Q8TSY0; Q8TSX9; Q8TSY4; Q8TSY3; Q8TSY1; Q8TSY2
the purified RnfG subunit fluoresces in SDS-PAGE gels under UV illumination and shows a UV-visible spectrum typical of flavoproteins. RnfG reveals a midpoint potential of -129 mV for FMN with n = 2
NAD+
-
Rnf's electron donation from NADH corresponds to inward flow of Na+. Subunit RnfC has an NADH binding motif
[4Fe-4S]-center
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
subunit RnfB contains 4Fe-4S clusters
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
K+
-
KCl itself has no effect on Na+ transport, in combination with valinomycin Na+ transport is stimulated slightly
Fe2+
-
[iron-sulfur] cluster, enzyme-bound in a polyferredoxin with four ferredoxin-like [4Fe-4S] centers in NfoB (RnfB)
Fe2+
-
[iron-sulfur] cluster, enzyme-bound in a polyferredoxin with four ferredoxin-like [4Fe-4S] centers in NfoB (RnfB)
Fe2+
-
[iron-sulfur] cluster, enzyme-bound in a polyferredoxin with four ferredoxin-like [4Fe-4S] centers in NfoB (RnfB)
Fe2+
-
subunits RnfB and RnfC each contain the sequence motif for an iron-sulfur center
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diphenyleniodonium chloride
-
complete inhibition of Na+ transport at 0.04 mM
diphenyliodonium chloride
-
complete inhibition of Na+ transport at 0.04 mM
N,N'-dicyclohexylcarbodiimide
-
inhibits ferredoxin:NAD+ oxidoreductase activity
additional information
-
the enzyme complex is inhibited by sodium ionophores but not protonophores, demonstrating a direct coupling of the ferredoxin:NAD+ oxidoreductase activity to Na+ transport
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ETH2120
-
reduced ferredoxin:NAD+ oxidoreductase activity at inverted membrane vesicles is not stimulated to 155% of control
monensin
-
reduced ferredoxin:NAD+ oxidoreductase activity at inverted membrane vesicles is not stimulated to 138% of control
valinomycin
-
reduced ferredoxin:NAD+ oxidoreductase activity at inverted membrane vesicles is not stimulated to 128% of control
valinomycin
-
in combination with K+, Na+ transport is stimulated slightly
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00026
reduced ferredoxin [iron-sulfur] cluster
-
at pH 6.8, temperature not specified in the publication
-
0.00042
reduced flavodoxin [iron-sulfur] cluster
-
at pH 6.8, temperature not specified in the publication
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.155
1,10-phenanthroline
Acetobacterium woodii
-
pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity
0.00375
Ag+
Acetobacterium woodii
-
pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity
0.00175
Cu2+
Acetobacterium woodii
-
pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity
0.000035
diphenyleniodonium chloride
Acetobacterium woodii
-
pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity
0.001
diphenyliodonium chloride
Acetobacterium woodii
-
pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from a highly enriched culture obtained from the intestinal tract of termites
-
-
brenda
isolated from a highly enriched culture obtained from the intestinal tract of termites
-
-
brenda
Q8TSY0 i.e. RnfA, Q8TSX9 i.e. RnfB, Q8TSY4 i.e. RnfC, Q8TSY3 i.e. RnfD, Q8TSY1 i.e. RnfE, Q8TSY2 i.e. RnfG
Q8TSY0; Q8TSX9; Q8TSY4; Q8TSY3; Q8TSY1; Q8TSY2
UniProt
brenda
C4N8U0: electron transport complex subunit C, C4N8U1: electron transport complex subunit D, C4N8U2: electron transport complex subunit G, C4N8U3: electron transport complex subunit E, C4N8U4: electron transport complex subunit A, C4N8U5: electron transport complex subunit B
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
UniProt
brenda
H6LC28 i.e. RnfA, H6LC27 i.e. RnfB, i.e. RnfC, H6LC31 i.e. RnfD, H6LC29 i.e. RnfE, H6LC30 i.e. RnfG
UniProt
brenda
H6LC28 i.e. RnfA, H6LC27 i.e. RnfB, i.e. RnfC, H6LC31 i.e. RnfD, H6LC29 i.e. RnfE, H6LC30 i.e. RnfG
UniProt
brenda
Q8TSY0 i.e. RnfA, Q8TSX9 i.e. RnfB, Q8TSY4 i.e. RnfC, Q8TSY3 i.e. RnfD, Q8TSY1 i.e. RnfE, Q8TSY2 i.e. RnfG
Q8TSY0; Q8TSX9; Q8TSY4; Q8TSY3; Q8TSY1; Q8TSY2
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
-
-
brenda
additional information
Q8TSY0; Q8TSX9; Q8TSY4; Q8TSY3; Q8TSY1; Q8TSY2
recombinant subunit RnfG, the C-terminal domain containing FMN is located on the outer aspect of the cytoplasmic membrane
brenda
-
recombinant subunit RnfG, the C-terminal domain containing FMN is located on the outer aspect of the cytoplasmic membrane
-
brenda
additional information
-
the flavins in RnfG and RnfD are localized in the periplasmic space
-
brenda
additional information
Vibrio cholerae serotype O1 O395N-1
-
the flavins in RnfG and RnfD are localized in the periplasmic space
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
iron limitation in Rhodobacter capsulatus leads to an increase in cellular levels of RnfB
metabolism
physiological function
additional information
evolution
acetogens can be divided into two groups, the Na+-dependent ones with Acetobacterium woodii and the H+-dependent ones with Moorella thermoacetica (formerly Clostridium thermoaceticum) as model organisms
evolution
-
the archaeon Methanosarcina acetivorans shows a variation of a Rnf complex where the rnf gene cluster has eight genes, one additional gene encodes for cytochrome c
evolution
-
acetogens can be divided into two groups, the Na+-dependent ones with Acetobacterium woodii and the H+-dependent ones with Moorella thermoacetica (formerly Clostridium thermoaceticum) as model organisms
-
metabolism
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport
metabolism
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
the constitutive production argues for an involvement of the Rnf complex not only in caffeate respiration but also in general metabolism
metabolism
-
the enzyme complex is involved in Na+-motive, anaerobic respiration with caffeate as electron acceptor
metabolism
-
methanogenesis from acetate by Methanosarcina acetivorans involves an anaerobic electron transport chain with ferredoxin as electron donor and heterodisulfide as electron acceptor. Proposed model of the aceticlastic pathway of methanogenesis in Methanosarcina acetivorans, overview
metabolism
-
possible involvement of the Rnf complex in the electron flow in the Wood-Ljungdahl pathway
metabolism
role of the enzyme Rnf complex in the Wood-Ljungdahl pathway, overview. Acetogens use the WoodLjungdahl pathway for reduction of carbon dioxide to acetate. This pathway not only allows reoxidation of reducing equivalents during heterotrophic growth but also supports chemolithoautotrophic growth on H2 +CO2. In addition to CO2, acetogens can use alternative electron acceptors, such as nitrate or caffeate. Caffeate respiration in the model acetogen Acetobacterium woodii is coupled to energy conservation via a chemiosmotic mechanism, with Na+ as coupling ion. Coupling of the Wood-Ljungdahl pathway to primary and electrogenic translocation of Na+ across the cytoplasmic membrane in Acetobacterium woodii
metabolism
Acetobacterium woodii DSM 103
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport
-
metabolism
-
electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport
-
metabolism
-
role of the enzyme Rnf complex in the Wood-Ljungdahl pathway, overview. Acetogens use the WoodLjungdahl pathway for reduction of carbon dioxide to acetate. This pathway not only allows reoxidation of reducing equivalents during heterotrophic growth but also supports chemolithoautotrophic growth on H2 +CO2. In addition to CO2, acetogens can use alternative electron acceptors, such as nitrate or caffeate. Caffeate respiration in the model acetogen Acetobacterium woodii is coupled to energy conservation via a chemiosmotic mechanism, with Na+ as coupling ion. Coupling of the Wood-Ljungdahl pathway to primary and electrogenic translocation of Na+ across the cytoplasmic membrane in Acetobacterium woodii
-
physiological function
-
enzymes of the Rnf family are bacterial redox-driven ion pumps, coupling an oxidoreduction process to the translocation of Na+ across the cell membrane
physiological function
-
in cells grown on acetate the rnf complex mediates oxidation of reduced ferredoxin (generated during acetyl-CoA oxidation) with reduction of methanophenanzine that then reduces the heterodisulfide
physiological function
-
RnfE might represent the coupling site for sodium ion translocation, the Rnf complex is involved in ferredoxin reduction in the bacterium
physiological function
the enzyme couples oxidation of reduced ferredoxin (generated by hydrogenase) with the reduction of NAD+. The Na+-translocating enzyme catalyzes electron transfer from ferredoxin to NAD+ coupled to electrogenic ion transport across the membrane. The enzyme is also involved in the electron-transfer pathway in caffeate respiration
physiological function
-
the physiological function is the reoxidation of reduced ferredoxin derived from pyruvate oxidation coupled to NAD+ reduction and Na+ export. The NADH generated is used as reductant in butyrate fermentation. Na+ is translocated through subunit RnfE
physiological function
-
the Rnf complex is a multi-subunit membrane-bound electron transport protein complex that is assumed to couple ferredoxin-dependent NAD+ reduction in bacteria with the translocation of ions across the cytoplasmic membrane. The electron transport during aceticlastic methanogenesis by Methanosarcina acetivorans involves a sodium-translocating Rnf complex, overview
physiological function
-
the Rnf complex is involved in ferredoxin reduction in the synthrophic bacterium. When growing on benzoate or fatty acids, this organism has to synthesize pyruvate from acetyl-CoA and CO2. The ferredoxin required might be generated via reversed electron flow from NADH driven by the transmembrane electrochemical ion (H+,Na+) gradient
physiological function
-
the Rnf complex may have a central role in the bioenergetics of Acetobacterium woodii. Oxidation of pyruvate (glycolysis) or H2 (chemolithoautotrophic growth) yields reduced ferredoxin. Electrons are wired to NAD+ by Rnf thereby generating a Na+-potential. Depending on the availability of electron acceptors, either CO2 or caffeate is reduced, overview
physiological function
-
all Methanomassiliicoccales strains possess a complex that is related to the F420:methanophenazine oxidoreductase (Fpo) of Methanosarcinales but lacks an F420-oxidizing module, resembling the apparently ferredoxin-dependent Fpo-like homolog in Methanosaeta thermophila. Since all Methanomassiliicoccales also lack the subunit E of the membrane-bound heterodisulfide reductase (HdrDE), ist seems that the Fpo-like complex interacts directly with subunit D, forming an energy-converting ferredoxin:heterodisulfide oxidoreductase. The dual function of heterodisulfide in Methanomassiliicoccales, which serves both in electron bifurcation and as terminal acceptor in a membrane-associated redox process, may be a unique characteristic of the distict order. Mechanism of energy conversion in the energy-converting ferredoxin:heterodisulfide oxidoreductase (Fpo-like/HdrD) complex, overview
physiological function
endergonic reduction of ferredoxin with NADH is driven by reverse electron transport catalyzed by the Rnf complex. Deletion of subunits RnfABCDEG results in a mutant that does not grow on H2 plus CO2, nor does it produce acetate or ATP from H2 plus CO2, and ferredoxin:NADx02 oxidoreductase activity and Na+ translocation are also completely lost. The mutant also does not grow on low-energy substrates, such as ethanol or lactate
physiological function
-
incorporation of a His-tagged variant of the ferredoxin:NAD oxidoreductase (Rnf complex) into artificial liposomes. The complex catalyzes Na+ transport coupled to ferredoxin-dependent NAD reduction. The Rnf complex is Na+-dependent, and creates a Na+ gradient across the membrane which can be used for ATP synthesis
physiological function
-
the Rnf complex is a primary Na+ pump. Together with a Na+-F1FO ATP synthase it builds a simple, two-limb respiratory chain in Thermotoga maritima
physiological function
-
incorporation of a His-tagged variant of the ferredoxin:NAD oxidoreductase (Rnf complex) into artificial liposomes. The complex catalyzes Na+ transport coupled to ferredoxin-dependent NAD reduction. The Rnf complex is Na+-dependent, and creates a Na+ gradient across the membrane which can be used for ATP synthesis
-
physiological function
-
the Rnf complex is a primary Na+ pump. Together with a Na+-F1FO ATP synthase it builds a simple, two-limb respiratory chain in Thermotoga maritima
-
physiological function
Vibrio cholerae serotype O1 O395N-1
-
enzymes of the Rnf family are bacterial redox-driven ion pumps, coupling an oxidoreduction process to the translocation of Na+ across the cell membrane
-
physiological function
-
all Methanomassiliicoccales strains possess a complex that is related to the F420:methanophenazine oxidoreductase (Fpo) of Methanosarcinales but lacks an F420-oxidizing module, resembling the apparently ferredoxin-dependent Fpo-like homolog in Methanosaeta thermophila. Since all Methanomassiliicoccales also lack the subunit E of the membrane-bound heterodisulfide reductase (HdrDE), ist seems that the Fpo-like complex interacts directly with subunit D, forming an energy-converting ferredoxin:heterodisulfide oxidoreductase. The dual function of heterodisulfide in Methanomassiliicoccales, which serves both in electron bifurcation and as terminal acceptor in a membrane-associated redox process, may be a unique characteristic of the distict order. Mechanism of energy conversion in the energy-converting ferredoxin:heterodisulfide oxidoreductase (Fpo-like/HdrD) complex, overview
-
physiological function
-
the enzyme couples oxidation of reduced ferredoxin (generated by hydrogenase) with the reduction of NAD+. The Na+-translocating enzyme catalyzes electron transfer from ferredoxin to NAD+ coupled to electrogenic ion transport across the membrane. The enzyme is also involved in the electron-transfer pathway in caffeate respiration
-
physiological function
-
endergonic reduction of ferredoxin with NADH is driven by reverse electron transport catalyzed by the Rnf complex. Deletion of subunits RnfABCDEG results in a mutant that does not grow on H2 plus CO2, nor does it produce acetate or ATP from H2 plus CO2, and ferredoxin:NADx02 oxidoreductase activity and Na+ translocation are also completely lost. The mutant also does not grow on low-energy substrates, such as ethanol or lactate
-
additional information
-
the ATP synthase of Acetobacterium woodii is a Na+ F1FO ATP synthase, structure analysis, overview
additional information
-
the Rnf complex of Methanosarcina acetivorans is suggested to reduce methanophenazine, which requires a different module compared to an enzyme that reduces NAD+. That may be the reason why this Rnf complex has a cytochrome c in addition
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RNFA_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
192
6
20434
Swiss-Prot
-
RNFB_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
333
1
34727
Swiss-Prot
-
RNFG_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
207
1
21832
Swiss-Prot
-
RNFE_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
196
5
20533
Swiss-Prot
-
RNFD_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
318
5
33739
Swiss-Prot
-
RNFC_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
443
0
47120
Swiss-Prot
-
A0A2U3KGR9_9FIRM
252
5
26944
TrEMBL
-
H6LBX7_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
654
0
71006
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21400
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
21600
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
22800
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
26000
-
1 * 26000, recombinant isolated subunit RnfG, SDS-PAGE, 1 * 39000, recombinant isolated subunit RnfD, SDS-PAGE
35000
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
36600
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
39000
-
1 * 26000, recombinant isolated subunit RnfG, SDS-PAGE, 1 * 39000, recombinant isolated subunit RnfD, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
the enzyme complex is composed of at least six different subunits, x * 35000 (subunit RnfD), x * 22800 (subunit RnfG), x * 21600 (subunit RnfE), x * 21400 (subunit RnfA), x * 36600 (subunit RnfB), calculated from sequence
dodecamer
hexamer
monomer
dodecamer
-
and hexamer, 2 * 10560, subunit RnfB, 2 * 34600, subunit RnfD, 2 * 24300, subunit RnfG, plus 2 * each of subunits RnfA, RnfC, RnfE, calculated from sequence and SDS-PAGE
dodecamer
-
and hexamer, 2 * 10560, subunit RnfB, 2 * 34600, subunit RnfD, 2 * 24300, subunit RnfG, plus 2 * each of subunits RnfA, RnfC, RnfE, calculated from sequence and SDS-PAGE
-
hexamer
-
the Rnf complex has six subunits, NfoABCDEG (Nfo is homologous to Rnf and stands for NADH:ferredoxinoxidoreductase)
hexamer
-
1 * 21400, subunit RnfA, 1 * 36600, subunit RnfB, 1 * 50000, subunit RnfC, 1 * 35000, subunit RnfD, 1 * 21600, subunit RnfE, 1 * 30000, subunit RnfG, respectively, SDS-PAGE
hexamer
-
and dodecamer, 1 * 10560, subunit RnfB, 1 * 34600, subunit RnfD, 1 * 24300, subunit RnfG, plus 1 subunits RnfA, RnfC, RnfE, calculated from sequence and SDS-PAGE
hexamer
-
1 * 21400, subunit RnfA, 1 * 36600, subunit RnfB, 1 * 50000, subunit RnfC, 1 * 35000, subunit RnfD, 1 * 21600, subunit RnfE, 1 * 30000, subunit RnfG, respectively, SDS-PAGE
-
hexamer
-
and dodecamer, 1 * 10560, subunit RnfB, 1 * 34600, subunit RnfD, 1 * 24300, subunit RnfG, plus 1 subunits RnfA, RnfC, RnfE, calculated from sequence and SDS-PAGE
-
hexamer
-
six subunits, RnfA, RnfB, RnfC, RnfD, RnfG, and RnfE, that include several conserved sequence motifs indicating the binding of redox cofactors: RnfC has an NADH binding motif, RnfB and RnfC each contain the sequence motif for an iron-sulfur center
hexamer
Vibrio cholerae serotype O1 O395N-1
-
six subunits, RnfA, RnfB, RnfC, RnfD, RnfG, and RnfE, that include several conserved sequence motifs indicating the binding of redox cofactors: RnfC has an NADH binding motif, RnfB and RnfC each contain the sequence motif for an iron-sulfur center
-
monomer
-
1 * 26000, recombinant isolated subunit RnfG, SDS-PAGE, 1 * 39000, recombinant isolated subunit RnfD, SDS-PAGE
monomer
Vibrio cholerae serotype O1 O395N-1
-
1 * 26000, recombinant isolated subunit RnfG, SDS-PAGE, 1 * 39000, recombinant isolated subunit RnfD, SDS-PAGE
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T166G
T175L
-
site-directed mutagenesis of subunit RnfG, the mutation affects FMN cofactor binding
T187V
-
site-directed mutagenesis of subunit RnfD, the mutation affects flavin cofactor binding
T278L
-
site-directed mutagenesis of subunit RnfD, the mutation does not affect flavin cofactor binding
T175L
Vibrio cholerae serotype O1 O395N-1
-
site-directed mutagenesis of subunit RnfG, the mutation affects FMN cofactor binding
-
T187V
Vibrio cholerae serotype O1 O395N-1
-
site-directed mutagenesis of subunit RnfD, the mutation affects flavin cofactor binding
-
T278L
Vibrio cholerae serotype O1 O395N-1
-
site-directed mutagenesis of subunit RnfD, the mutation does not affect flavin cofactor binding
-
T166G
Q8TSY0; Q8TSX9; Q8TSY4; Q8TSY3; Q8TSY1; Q8TSY2
variant of subunit RnfG, contrary to wild-type, variant is colorless and fails to fluoresce under UV illumination
T166G
-
variant of subunit RnfG, contrary to wild-type, variant is colorless and fails to fluoresce under UV illumination
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purifiaction under strictly anoxic conditions. Solubilization is achieved with n-dodecyl beta-D-maltoside, followed by anion exchange chromatography on Q-sepharose and gel filtration on Sephacryl S300
-
recombinant wild-type and mutant His-tagged RnfD and RnfG fom Vibrio cholerae cells by nickel affinity chromatography and gel filtration
-
Rnf complex with 6 components
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree and analysis
-
expression of the Rnf cpmplex and of subunit RnfC and RnfB alone in Escherichia coli
-
genes rnfD and rnfG, cloning of Rnf complex subunits and recombinant individual expression of wild-type and mutant His-tagged RnfD and RnfG in Vibrio cholerae cells producing protein fluorescence under UV illumination, recombinant subunit protein topology analysis, overview
-
RnfC and RnfG are overproduced in Escherichia coli
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hess, V.; Schuchmann, K.; Mller, V.
The ferredoxin: NAD+ oxidoreductase (Rnf) from the acetogen Acetobacterium woodii requires Na+ and is reversibly coupled to the membrane potential
J. Biol. Chem.
288
31496-31502
2013
Acetobacterium woodii, Acetobacterium woodii DSM 1030
brenda
Biegel, E.; Schmidt, S.; Mller, V.
Genetic, immunological and biochemical evidence for a Rnf complex in the acetogen Acetobacterium woodii
Environ. Microbiol.
11
1438-1443
2009
Acetobacterium woodii (C4N8U0 and C4N8U1 and C4N8U2 and C4N8U3 and C4N8U4 and C4N8U5), Acetobacterium woodii
brenda
Biegel, E.; Mller, V.
Bacterial Na+-translocating ferredoxin:NAD+ oxidoreductase
Proc. Natl. Acad. Sci. USA
107
18138-18142
2010
Acetobacterium woodii
brenda
Mueller, V.; Imkamp, F.; Biegel, E.; Schmidt, S.; Dilling, S.
Discovery of a ferredoxin:NAD+-oxidoreductase (Rnf) in Acetobacterium woodii: A novel potential coupling site in acetogens
Ann. N. Y. Acad. Sci.
1125
137-146
2008
Azotobacter vinelandii, Clostridium tetani, Clostridium tetanomorphum, Rhodobacter capsulatus, Syntrophus aciditrophicus, Methanosarcina acetivorans, Acetobacterium woodii (H6LBX7), Acetobacterium woodii, Acetobacterium woodii DSM 1030 (H6LBX7)
brenda
Backiel, J.; Juárez, O.; Zagorevski, D.; Wang, Z.; Nilges, M.; Barquera, B.
Covalent binding of flavins to RnfG and RnfD in the Rnf complex from Vibrio cholerae
Biochemistry
47
11273-11284
2008
Vibrio cholerae serotype O1, Vibrio cholerae serotype O1 O395N-1
brenda
Schmidt, S.; Biegel, E.; Mueller, V.
The ins and outs of Na+ bioenergetics in Acetobacterium woodii
Biochim. Biophys. Acta
1787
691-696
2009
Acetobacterium woodii
brenda
Schlegel, K.; Welte, C.; Deppenmeier, U.; Mueller, V.
Electron transport during aceticlastic methanogenesis by Methanosarcina acetivorans involves a sodium-translocating Rnf complex
FEBS J.
279
4444-4452
2012
Methanosarcina acetivorans
brenda
Lang, K.; Schuldes, J.; Klingl, A.; Poehlein, A.; Daniel, R.; Brunea, A.
New mode of energy metabolism in the seventh order of methanogens as revealed by comparative genome analysis of Candidatus methanoplasma termitum
Appl. Environ. Microbiol.
81
1338-1352
2015
Candidatus Methanoplasma termitum, Candidatus Methanoplasma termitum MpT1
brenda
Chowdhury, N.P.; Klomann, K.; Seubert, A.; Buckel, W.
Reduction of flavodoxin by electron bifurcation and sodium ion-dependent reoxidation by NAD+ catalyzed by ferredoxin-NAD+ reductase (Rnf)
J. Biol. Chem.
291
11993-12002
2016
Acidaminococcus fermentans, Acidaminococcus fermentans VR4
brenda
Kuhns, M.; Schuchmann, V.; Schmidt, S.; Friedrich, T.; Wiechmann, A.; Mueller, V.
The Rnf complex from the acetogenic bacterium Acetobacterium woodii Purification and characterization of RnfC and RnfB
Biochim. Biophys. Acta
1861
148263
2020
Thermotoga maritima, Thermotoga maritima DSM 3109
brenda
Wiechmann, A.; Trifunovic, D.; Klein, S.; Mueller, V.
Homologous production, one-step purification, and proof of Na+ transport by the Rnf complex from Acetobacterium woodii, a model for acetogenic conversion of C1 substrates to biofuels
Biotechnol. Biofuels
13
208
2020
Thermotoga maritima, Thermotoga maritima DSM 3109
brenda
Kuhns, M.; Trifunovic, D.; Huber, H.; Mueller, V.
The Rnf complex is a Na+ coupled respiratory enzyme in a fermenting bacterium, Thermotoga maritima
Commun. Biol.
3
431
2020
Thermotoga maritima, Thermotoga maritima DSM 3109
brenda
Westphal, L.; Wiechmann, A.; Baker, J.; Minton, N.; Mueller, V.
The Rnf complex is an energy-coupled transhydrogenase essential to reversibly link cellular NADH and ferredoxin pools in the acetogen Acetobacterium woodii
J. Bacteriol.
200
e00357
2018
Acetobacterium woodii (H6LC28 and H6LC27 and H6LC32 and H6LC31 and H6LC29 and H6LC30), Acetobacterium woodii, Acetobacterium woodii DSM 1030 (H6LC28 and H6LC27 and H6LC32 and H6LC31 and H6LC29 and H6LC30)
brenda
Suharti, S.; Wang, M.; de Vries, S.; Ferry, J.G.
Characterization of the RnfB and RnfG subunits of the Rnf complex from the archaeon Methanosarcina acetivorans
PLoS ONE
9
e97966
2014
Methanosarcina acetivorans (Q8TSY0 and Q8TSX9 and Q8TSY4 and Q8TSY3 and Q8TSY1 and Q8TSY2), Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834 (Q8TSY0 and Q8TSX9 and Q8TSY4 and Q8TSY3 and Q8TSY1 and Q8TSY2)
brenda
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EXTERNAL LINKS (specific for EC-Number 7.2.1.2)
Transporter Classification Database (TCDB): 3.D.6.1.2
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Release 2023.1 (January 2023)
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