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Literature summary extracted from

  • Brueggemann, H.; Falinski, F.; Deppenmeier, U.
    Structure of the F420H2:quinone oxidoreductase of Archaeoglobus fulgidus identification and overproduction of the F420H2-oxidizing subunit (2000), Eur. J. Biochem., 267, 5810-5814.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.98.4 overexpressed in Escherichia coli Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.98.4 Iron-sulfur cluster the purified fqoF polypeptide contains 10.6 mol non-heme iron and 7.2 mol acid-labile sulfur per mol protein Archaeoglobus fulgidus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.98.4 39000
-
x * 39000 (subunit FqoF), SDS-PAGE. The F420H2:quinone oxidoreductase may be composed of three subcomplexes. The purified subunit FqoF oxidizes reduced cofactor F420 using the electron-acceptor system methyl viologen plus metronidazole. The subunits FqoB, FqoCD and FqoI may form the membrane-associated module and transfer electrons to the membrane-integral modulemodule. It is most likely that the last subcomplex is composed of FqoA, FqoH, FqoJ, FqoK, FqoL, FqoM and FqoN. All subunits are highly hydrophobic and are probably involved in the reduction of a special menaquinone with a fully reduced isoprenoid side chain present in the cytoplasmic membrane of Archaeoglobus fulgidus Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.98.4 menaquinone + reduced coenzyme F420 Archaeoglobus fulgidus the FqoF protein forms the input device of the protein complex which oxidizes coenzyme F420H2. Thus, this polypeptide replaces the NADH-oxidizing module of NADH dehydrogenases of bacteria which are not found in Archaeoglobus fulgidus. Then the electrons are channeled to the membrane-associated fragment composed of FqoBCDI, which is homologous to the corresponding module of complex I. As the subunits FqoAHJKLMN are highly hydrophobic and are related to polypeptides comprising the membrane fragment of complex I, they may form the membrane-integral module of the F420H2:quinone oxidoreductase that is responsible for the reduction of a special menaquinone found in the cytoplasmic membrane of Archaeoglobus fulgidus menaquinol + oxidized coenzyme F420
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.98.4 Archaeoglobus fulgidus O28443 FqoF subunit of the F420H2:quinone oxidoreductase
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.98.4
-
Archaeoglobus fulgidus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.98.4 0.21
-
pH 7, 22°C, crude extract, electron-acceptor system consisting of metronidazole and methyl viologen Archaeoglobus fulgidus
1.1.98.4 9.3
-
pH 7, 22°C, purified enzyme, electron-acceptor system consisting of metronidazole and methyl viologen Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.98.4 menaquinone + reduced coenzyme F420 the FqoF protein forms the input device of the protein complex which oxidizes coenzyme F420H2. Thus, this polypeptide replaces the NADH-oxidizing module of NADH dehydrogenases of bacteria which are not found in Archaeoglobus fulgidus. Then the electrons are channeled to the membrane-associated fragment composed of FqoBCDI, which is homologous to the corresponding module of complex I. As the subunits FqoAHJKLMN are highly hydrophobic and are related to polypeptides comprising the membrane fragment of complex I, they may form the membrane-integral module of the F420H2:quinone oxidoreductase that is responsible for the reduction of a special menaquinone found in the cytoplasmic membrane of Archaeoglobus fulgidus Archaeoglobus fulgidus menaquinol + oxidized coenzyme F420
-
?
1.1.98.4 oxidized methyl viologen + reduced coenzyme F420 the purified subunit oxidizes reduced cofactor F420 using the electron-acceptor system methyl viologen plus metronidazole Archaeoglobus fulgidus reduced methyl viologen + oxidized coenzyme F420
-
?

Subunits

EC Number Subunits Comment Organism
1.1.98.4 oligomer x * 39000 (subunit FqoF), SDS-PAGE. The F420H2:quinone oxidoreductase may be composed of three subcomplexes. The purified subunit FqoF oxidizes reduced cofactor F420 using the electron-acceptor system methyl viologen plus metronidazole. The subunits FqoB, FqoCD and FqoI may form the membrane-associated module and transfer electrons to the membrane-integral modulemodule. It is most likely that the last subcomplex is composed of FqoA, FqoH, FqoJ, FqoK, FqoL, FqoM and FqoN. All subunits are highly hydrophobic and are probably involved in the reduction of a special menaquinone with a fully reduced isoprenoid side chain present in the cytoplasmic membrane of Archaeoglobus fulgidus Archaeoglobus fulgidus

Synonyms

EC Number Synonyms Comment Organism
1.1.98.4 AF1833
-
Archaeoglobus fulgidus
1.1.98.4 FqoF protein subunit of the F420H2:quinone oxidoreductase Archaeoglobus fulgidus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.98.4 78
-
assay at Archaeoglobus fulgidus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.98.4 FAD the purified fqoF polypeptide contains 0.7 mol FAD per mol protein Archaeoglobus fulgidus

General Information

EC Number General Information Comment Organism
1.1.98.4 physiological function the FqoF protein forms the input device of the protein complex which oxidizes coenzyme F420H2. Thus, this polypeptide replaces the NADH-oxidizing module of NADH dehydrogenases of bacteria which are not found in Archaeoglobus fulgidus. Then the electrons are channeled to the membrane-associated fragment composed of FqoBCDI, which is homologous to the corresponding module of complex I. As the subunits FqoAHJKLMN are highly hydrophobic and are related to polypeptides comprising the membrane fragment of complex I, they may form the membrane-integral module of the F420H2:quinone oxidoreductase that is responsible for the reduction of a special menaquinone found in the cytoplasmic membrane of Archaeoglobus fulgidus Archaeoglobus fulgidus