Any feedback?
Information on EC 7.2.1.2 - ferredoxin-NAD+ oxidoreductase (Na+-transporting) and Organism(s) Acetobacterium woodii and UniProt Accession H6LC30
for references in articles please use BRENDA:EC7.2.1.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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 taxonomic range for the selected organisms is: Acetobacterium woodii
The expected taxonomic range for this enzyme is: Bacteria, Archaea
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ferredoxin:NAD+-oxidoreductase complex
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
-
Na+-translocating ferredoxin:NAD+-oxidoreductase
Rnf
Rnf complex
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.
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 + NAD+ + H+ + Na+[side 1]
2 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
-
-
-
-
?
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+[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]
-
-
-
?
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
-
-
?
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 + NAD+ + H+ + Na+[side 1]
2 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+[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]
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iron-sulfur centre
-
ironsulfur and flavin-containing electron transport complex
[4Fe-4S]-center
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
subunit RnfB contains 4Fe-4S clusters
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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
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
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
H6LC28 i.e. RnfA, H6LC27 i.e. RnfB, i.e. RnfC, H6LC31 i.e. RnfD, H6LC29 i.e. RnfE, H6LC30 i.e. RnfG
UniProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
-
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
additional information
-
the ATP synthase of Acetobacterium woodii is a Na+ F1FO ATP synthase, structure analysis, overview
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
-
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
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 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
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
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
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RnfC and RnfG are overproduced in Escherichia coli
C4N8U0; C4N8U1; C4N8U2; C4N8U3; C4N8U4; C4N8U5
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
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
Biegel, E.; Mller, V.
Bacterial Na+-translocating ferredoxin:NAD+ oxidoreductase
Proc. Natl. Acad. Sci. USA
107
18138-18142
2010
Acetobacterium woodii
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)
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
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)
EXTERNAL LINKS (specific for EC-Number 7.2.1.2)
Transporter Classification Database (TCDB): 3.D.6.1.2
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
