Cloned (Comment) | Organism |
---|---|
overexpressed in Escherichia coli | Archaeoglobus fulgidus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | O28443 | FqoF subunit of the F420H2:quinone oxidoreductase | - |
Purification (Comment) | Organism |
---|---|
- |
Archaeoglobus fulgidus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.21 | - |
pH 7, 22°C, crude extract, electron-acceptor system consisting of metronidazole and methyl viologen | Archaeoglobus fulgidus |
9.3 | - |
pH 7, 22°C, purified enzyme, electron-acceptor system consisting of metronidazole and methyl viologen | Archaeoglobus fulgidus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? | |
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 | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
AF1833 | - |
Archaeoglobus fulgidus |
FqoF protein | subunit of the F420H2:quinone oxidoreductase | Archaeoglobus fulgidus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
78 | - |
assay at | Archaeoglobus fulgidus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | the purified fqoF polypeptide contains 0.7 mol FAD per mol protein | Archaeoglobus fulgidus |
General Information | Comment | Organism |
---|---|---|
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 |