Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.1.2 Fe2+ [iron-sulfur] cluster Rhodobacter capsulatus
7.2.1.2 Fe2+ [iron-sulfur] cluster Acetobacterium woodii
7.2.1.2 Fe2+ [iron-sulfur] cluster, enzyme-bound Azotobacter vinelandii
7.2.1.2 Fe2+ [iron-sulfur] cluster, enzyme-bound Syntrophus aciditrophicus
7.2.1.2 Fe2+ [iron-sulfur] cluster, enzyme-bound in a polyferredoxin with four ferredoxin-like [4Fe-4S] centers in NfoB (RnfB) Clostridium tetanomorphum
7.2.1.2 Fe2+ [iron-sulfur] cluster, enzyme-bound in a polyferredoxin with four ferredoxin-like [4Fe-4S] centers in NfoB (RnfB) Clostridium tetani
7.2.1.2 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + methanophenazine + Na+[side 1] Methanosarcina acetivorans
-
 2 oxidized ferredoxin [iron-sulfur] cluster + reduced methanophenazine + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Rhodobacter capsulatus
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Azotobacter vinelandii
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Clostridium tetanomorphum
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Clostridium tetani
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Syntrophus aciditrophicus
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] Acetobacterium woodii
-
 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 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

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

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + methanophenazine + Na+[side 1]
-
 Methanosarcina acetivorans 2 oxidized ferredoxin [iron-sulfur] cluster + reduced methanophenazine + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Rhodobacter capsulatus 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Azotobacter vinelandii 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Clostridium tetanomorphum 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Clostridium tetani 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Syntrophus aciditrophicus 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1]
-
 Acetobacterium woodii 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
-
 ?
7.2.1.2 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]
-
 ?
7.2.1.2 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]
-
 ?
7.2.1.2 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 ?
-
 ?
7.2.1.2 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 DSM 1030 ?
-
 ?

Subunits

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

Synonyms

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

Cofactor

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

General Information

EC Number General Information Comment Organism
7.2.1.2 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
7.2.1.2 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
7.2.1.2 malfunction iron limitation in Rhodobacter capsulatus leads to an increase in cellular levels of RnfB Rhodobacter capsulatus
7.2.1.2 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
7.2.1.2 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
7.2.1.2 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
7.2.1.2 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
7.2.1.2 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
7.2.1.2 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
7.2.1.2 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