An enzyme complex that contains FAD and iron-sulfur clusters. The enzyme has been described in the archaea Methanosarcina mazei and Archaeoglobus fulgidus.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
quinol:coenzyme-F420 oxidoreductase
An enzyme complex that contains FAD and iron-sulfur clusters. The enzyme has been described in the archaea Methanosarcina mazei and 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
the physiological electron acceptor of the enzyme complex is most likely the menaquinone found in the membrane fraction of Archaeoglobus fulgidus. The reduction of menaquinone by F420H2 in Archaeoglobus fulgidus is catalyzed by a membrane-bound complex composed of at least seven different subunits. It contains 1-2 mol FAD and8 mol Fe-S/mol complex. The complex subunit composition indicates that the F420H2:quinone oxidoreductase complex from Archaeoglobus fulgidus is functionally analogous to the NADH:quinone oxidoreductase complex from mitochondria and bacteria
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
the physiological electron acceptor of the enzyme complex is most likely the menaquinone found in the membrane fraction of Archaeoglobus fulgidus. The reduction of menaquinone by F420H2 in Archaeoglobus fulgidus is catalyzed by a membrane-bound complex composed of at least seven different subunits. It contains 1-2 mol FAD and8 mol Fe-S/mol complex. The complex subunit composition indicates that the F420H2:quinone oxidoreductase complex from Archaeoglobus fulgidus is functionally analogous to the NADH:quinone oxidoreductase complex from mitochondria and bacteria
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
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity is almost stable in aerobic solutions. No activity is lost when 2 mg purified protein in 1 ml 50 mM Tricine/KOH, pH 7.5, containing 0.2% dodecyl-/I-D-maltoside is stored at 4°C for 6 h under air as the gas phase
F420H2: quinone oxidoreductase from Archaeoglobus fulgidus. Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters