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Literature summary for 7.2.1.2 extracted from

  • 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 (2008), Ann. N. Y. Acad. Sci., 1125, 137-146.
    View publication on PubMed
Search for more literature for 7.2.1.2

Cloned(Commentary)

Cloned (Comment) Organism
gene cluter rnfCDGEAB Clostridium tetani
gene rnfC, encoded in the rnfABCDEF cluster Rhodobacter capsulatus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound enzyme Acetobacterium woodii 16020
-
membrane tightly bound membrane-bound enzyme Rhodobacter capsulatus 16020
-
soluble RnfH might be a soluble protein Rhodobacter capsulatus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ [iron-sulfur] cluster Rhodobacter capsulatus
Fe2+ [iron-sulfur] cluster Acetobacterium woodii
Fe2+ [iron-sulfur] cluster, enzyme-bound Azotobacter vinelandii
Fe2+ [iron-sulfur] cluster, enzyme-bound Syntrophus aciditrophicus
Fe2+ [iron-sulfur] cluster, enzyme-bound in a polyferredoxin with four ferredoxin-like [4Fe-4S] centers in NfoB (RnfB) Clostridium tetanomorphum
Fe2+ [iron-sulfur] cluster, enzyme-bound in a polyferredoxin with four ferredoxin-like [4Fe-4S] centers in NfoB (RnfB) Clostridium tetani
Fe2+ [iron-sulfur] cluster, enzyme-bound in a polyferredoxin with four ferredoxin-like [4Fe-4S] centers in NfoB (RnfB) Methanosarcina acetivorans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 reduced ferredoxin [iron-sulfur] cluster + methanophenazine + Na+[side 1] Methanosarcina acetivorans
-
 2 oxidized ferredoxin [iron-sulfur] cluster + reduced methanophenazine + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Rhodobacter capsulatus
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Azotobacter vinelandii
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Clostridium tetanomorphum
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Clostridium tetani
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Syntrophus aciditrophicus
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Acetobacterium woodii
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Acetobacterium woodii DSM 1030
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?

Organism

Organism UniProt Comment Textmining
Acetobacterium woodii H6LBX7 subunit RnfC
-
Acetobacterium woodii DSM 1030 H6LBX7 subunit RnfC
-
Azotobacter vinelandii
-
 gene cluster rnf1 and rnf2
-
Clostridium tetani
-
 gene cluster rnfCDGEAB
-
Clostridium tetanomorphum
-
-
-
Methanosarcina acetivorans
-
 gene cluster rnfCDGEAB
-
Rhodobacter capsulatus
-
 rnfABCDEF gene cluster
-
Syntrophus aciditrophicus
-
 gene cluster rnf
-

Purification (Commentary)

Purification (Comment) Organism
Rnf complex with 6 components Azotobacter vinelandii
Rnf complex with 6 components Clostridium tetanomorphum
Rnf complex with 6 components Clostridium tetani
Rnf complex with 6 components Syntrophus aciditrophicus
Rnf complex with 6 components Methanosarcina acetivorans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin [iron-sulfur] cluster + methanophenazine + Na+[side 1]
-
 Methanosarcina acetivorans 2 oxidized ferredoxin [iron-sulfur] cluster + reduced methanophenazine + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Rhodobacter capsulatus 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Azotobacter vinelandii 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Clostridium tetanomorphum 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Clostridium tetani 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Syntrophus aciditrophicus 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Acetobacterium woodii 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] electron transfer from Fdred to NAD+ generates an Na+ potential Clostridium tetani 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Acetobacterium woodii DSM 1030 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 Acetobacterium woodii ?
-
 ?
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 Acetobacterium woodii DSM 1030 ?
-
 ?

Subunits

Subunits Comment Organism
hexamer the Rnf complex has six subunits, NfoABCDEG (Nfo is homologous to Rnf and stands for NADH:ferredoxinoxidoreductase) Clostridium tetanomorphum
hexamer the Rnf complex has six subunits, RnfABCDEG Azotobacter vinelandii
hexamer the Rnf complex has six subunits, RnfABCDEG Syntrophus aciditrophicus
hexamer the Rnf complex has six subunits, RnfCDGEAB Clostridium tetani
hexamer the Rnf complex has six subunits, RnfCDGEAB Methanosarcina acetivorans

Synonyms

Synonyms Comment Organism
Na+-translocating ferredoxin:NAD+-oxidoreductase
-
 Rhodobacter capsulatus
Na+-translocating ferredoxin:NAD+-oxidoreductase
-
 Azotobacter vinelandii
Na+-translocating ferredoxin:NAD+-oxidoreductase
-
 Clostridium tetanomorphum
Na+-translocating ferredoxin:NAD+-oxidoreductase
-
 Clostridium tetani
Na+-translocating ferredoxin:NAD+-oxidoreductase
-
 Syntrophus aciditrophicus
Na+-translocating ferredoxin:NAD+-oxidoreductase
-
 Methanosarcina acetivorans
Na+-translocating ferredoxin:NAD+-oxidoreductase
-
 Acetobacterium woodii
NADH:ferredoxin-oxidoreductase
-
 Clostridium tetanomorphum
Nfo
-
 Clostridium tetanomorphum
Rnf
-
 Acetobacterium woodii
Rnf complex
-
 Rhodobacter capsulatus
Rnf complex
-
 Clostridium tetanomorphum
Rnf complex
-
 Clostridium tetani
Rnf complex
-
 Syntrophus aciditrophicus
Rnf complex
-
 Methanosarcina acetivorans
Rnf complex
-
 Acetobacterium woodii
Rnf1 complex
-
 Azotobacter vinelandii
Rnf2 complex
-
 Azotobacter vinelandii

Cofactor

Cofactor Comment Organism Structure
cytochrome c
-
 Methanosarcina acetivorans
FAD bound to subunit RnfD Azotobacter vinelandii
FAD bound to subunit RnfD Clostridium tetanomorphum
FAD bound to subunit RnfD Clostridium tetani
FAD bound to subunit RnfD Syntrophus aciditrophicus
FAD bound to subunit RnfD Methanosarcina acetivorans
Ferredoxin
-
 Acetobacterium woodii
Ferredoxin bound to subunit RnfB Azotobacter vinelandii
Ferredoxin bound to subunit RnfB Clostridium tetanomorphum
Ferredoxin bound to subunit RnfB Clostridium tetani
Ferredoxin bound to subunit RnfB Syntrophus aciditrophicus
Ferredoxin bound to subunit RnfB Methanosarcina acetivorans
Ferredoxin RnfC contains two [4Fe-4S]-type ferredoxin-like domains Rhodobacter capsulatus
flavin noncovalently and covalently bound flavins in a polyferredoxin with four ferredoxin-like [4Fe-4S] centers in NfoB (RnfB) Clostridium tetanomorphum
FMN bound to subunit RnfC Azotobacter vinelandii
FMN bound to subunit RnfC Clostridium tetanomorphum
FMN bound to subunit RnfC Clostridium tetani
FMN bound to subunit RnfC Syntrophus aciditrophicus
FMN bound to subunit RnfC Methanosarcina acetivorans
FMN the binding site is located in subunit RnfG Rhodobacter capsulatus
methanophenazine
-
 Methanosarcina acetivorans
NAD+
-
 Rhodobacter capsulatus
NAD+
-
 Azotobacter vinelandii
NAD+
-
 Clostridium tetanomorphum
NAD+
-
 Clostridium tetani
NAD+
-
 Syntrophus aciditrophicus
NAD+
-
 Acetobacterium woodii

General Information

General Information Comment Organism
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 Acetobacterium woodii
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 Methanosarcina acetivorans
malfunction iron limitation in Rhodobacter capsulatus leads to an increase in cellular levels of RnfB Rhodobacter capsulatus
metabolism role of the enzyme Rnf complex in the Wood-Ljungdahl pathway, overview. Acetogens use the Wood–Ljungdahl 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 Acetobacterium woodii
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 Methanosarcina acetivorans
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 Methanosarcina acetivorans
physiological function RnfE might represent the coupling site for sodium ion translocation, the Rnf complex is involved in ferredoxin reduction in the bacterium Rhodobacter capsulatus
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 Acetobacterium woodii
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 Clostridium tetani
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 Syntrophus aciditrophicus