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Literature summary for 7.1.1.2 extracted from
- Energy-converting respiratory Complex I: on the way to the molecular mechanism of the proton pump (2013), Int. J. Biochem. Cell Biol., 45, 491-511.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Thermus thermophilus | 16020 | - |
| membrane | - |
Escherichia coli | 16020 | - |
| mitochondrial inner membrane | - |
Yarrowia lipolytica | 5743 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | 8-9 FeS clusters per enzyme molecule, 8 of which are organized as a continuous eT chain connecting FMN and a ubiquinone binding site. Thermodynamic properties of FeS clusters, overview | Thermus thermophilus |  |
| Fe2+ | 8-9 FeS clusters per enzyme molecule, 8 of which are organized as a continuous eT chain connecting FMN and a ubiquinone binding site. Thermodynamic properties of FeS clusters, overview | Escherichia coli | |
| Fe2+ | 8-9 FeS clusters per enzyme molecule, 8 of which are organized as a continuous eT chain connecting FMN and a ubiquinone binding site. Thermodynamic properties of FeS clusters, overview | Yarrowia lipolytica | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| NADH + ubiquinone + 6 H+[side 1] | Escherichia coli | - |
NAD+ + ubiquinol + 7 H+[side 2] | - |
? | |
| NADH + ubiquinone + 6 H+[side 1] | Yarrowia lipolytica | - |
NAD+ + ubiquinol + 7 H+[side 2] | - |
? | |
| NADH + ubiquinone + 6 H+[side 1] | Thermus thermophilus | electron transfer path from FMN to ubiquinone through the FeS cluster chain. Upon the oxidation of one NADH molecule 4H+ are translocated across the membrane from N-side (cytoplasm, equivalent to the mitochondrial matrix) to P-side (periplasm, equivalent to the mitochondrial intermembrane space) | NAD+ + ubiquinol + 7 H+[side 2] | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Thermus thermophilus | - |
- |
- |
| Yarrowia lipolytica | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| NADH + ubiquinone + 6 H+[side 1] | - |
Thermus thermophilus | NAD+ + ubiquinol + 7 H+[side 2] | - |
? | |
| NADH + ubiquinone + 6 H+[side 1] | - |
Escherichia coli | NAD+ + ubiquinol + 7 H+[side 2] | - |
? | |
| NADH + ubiquinone + 6 H+[side 1] | - |
Yarrowia lipolytica | NAD+ + ubiquinol + 7 H+[side 2] | - |
? | |
| NADH + ubiquinone + 6 H+[side 1] | electron transfer path from FMN to ubiquinone through the FeS cluster chain. Upon the oxidation of one NADH molecule 4H+ are translocated across the membrane from N-side (cytoplasm, equivalent to the mitochondrial matrix) to P-side (periplasm, equivalent to the mitochondrial intermembrane space) | Thermus thermophilus | NAD+ + ubiquinol + 7 H+[side 2] | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | two domains, hydrophilic and hydrophobic, constitute Complex I. The hydrophilic domain of Complex I contains noncovalently bound FMN and 8-9 FeS clusters, 8 of which are organized as a continuous eT chain connecting FMN and a UQ binding site. One or two UQ-binding sites are located at the interface between the hydrophilic and membrane Complex I domains or in the membrane domain close to the interface area. The hydrophilic domain is composed of 6 or 7 core subunits and protrudes to cytoplasm or mitochondrial matrix. The substrate binding site is located in the open cleft on the surface of the protein. The conserved residues aligning this solvent-accessible cavity form an unusual Rossmann fold, which provides tight packing of the substrate, ensures the planar condensed system of the nicotinamide and the FMN isoalloxazine rings and therefore determines high affinity to NADH, substrate specificity and high rate of hydride transfer to FMN | Yarrowia lipolytica |
| More | two domains, hydrophilic and hydrophobic, constitute Complex I. The hydrophilic domain of Complex I contains noncovalently bound FMN and 8-9 FeS clusters, 8 of which are organized as a continuous eT chain connecting FMN and a UQ binding site. One or two UQ-binding sites are located at the interface between the hydrophilic and membrane Complex I domains or in the membrane domain close to the interface area. The hydrophilic domain is composed of 6 or 7 core subunits and protrudes to cytoplasm or mitochondrial matrix. The substrate binding site is located in the open cleft on the surface of the protein. The conserved residues aligning this solvent-accessible cavity form an unusual Rossmann fold, which provides tight packing of the substrate, ensures the planar condensed system of the nicotinamide and the FMN isoalloxazine rings and therefore determines high affinity to NADH, substrate specificity and high rate of hydride transfer to FMN. The membrane domain of bacterial Complex I consists of 7 subunits equivalent to core subunits of mitochondrial enzyme | Thermus thermophilus |
| More | two domains, hydrophilic and hydrophobic, constitute Complex I. The hydrophilic domain of Complex I contains noncovalently bound FMN and 8-9 FeS clusters, 8 of which are organized as a continuous eT chain connecting FMN and a UQ binding site. One or two UQ-binding sites are located at the interface between the hydrophilic and membrane Complex I domains or in the membrane domain close to the interface area. The hydrophilic domain is composed of 6 or 7 core subunits and protrudes to cytoplasm or mitochondrial matrix. The substrate binding site is located in the open cleft on the surface of the protein. The conserved residues aligning this solvent-accessible cavity form an unusual Rossmann fold, which provides tight packing of the substrate, ensures the planar condensed system of the nicotinamide and the FMN isoalloxazine rings and therefore determines high affinity to NADH, substrate specificity and high rate of hydride transfer to FMN. The membrane domain of bacterial Complex I consists of 7 subunits equivalent to core subunits of mitochondrial enzyme | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| complex I | - |
Thermus thermophilus |
| complex I | - |
Escherichia coli |
| complex I | - |
Yarrowia lipolytica |
| NADH:ubiquinone oxidoreductase | - |
Thermus thermophilus |
| NADH:ubiquinone oxidoreductase | - |
Escherichia coli |
| NADH:ubiquinone oxidoreductase | - |
Yarrowia lipolytica |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FMN | noncovalently bound | Thermus thermophilus | |
| FMN | noncovalently bound | Escherichia coli | |
| FMN | noncovalently bound | Yarrowia lipolytica | |
| NADH | - |
Thermus thermophilus | |
| NADH | - |
Escherichia coli | |
| NADH | - |
Yarrowia lipolytica | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | bacterial Complex I is about half the size of the mitochondrial enzyme and is composed of only 13, in Escherichia coli, subunits representing a minimum functional version of the mitochondrial enzyme and performing the same function of coupling redox reaction to proton translocation. Prokaryotic Complex I is much more fragile than the eukaryotic mitochondrial enzyme | Thermus thermophilus |
| evolution | bacterial Complex I is about half the size of the mitochondrial enzyme and is composed of only 13, in Escherichia coli, subunits representing a minimum functional version of the mitochondrial enzyme and performing the same function of coupling redox reaction to proton translocation. Prokaryotic Complex I is much more fragile than the eukaryotic mitochondrial enzyme | Escherichia coli |
| evolution | bacterial Complex I is about half the size of the mitochondrial enzyme and is composed of only 13, in Escherichia coli, subunits representing a minimum functional version of the mitochondrial enzyme of eukaryotes and performing the same function of coupling redox reaction to proton translocation. Prokaryotic Complex I is much more fragile than the eukaryotic mitochondrial enzyme | Yarrowia lipolytica |
| additional information | potential energy profile for the Complex I substrates and cofactors, overview | Thermus thermophilus |
| additional information | potential energy profile for the Complex I substrates and cofactors, overview | Escherichia coli |
| additional information | potential energy profile for the Complex I substrates and cofactors, overview. Redox potentials of mitochondrial respiratory complexes, overview. Two domains, hydrophilic and hydrophobic, constitute Complex I. The hydrophilic domain of Complex I contains noncovalently bound FMN and 8-9 FeS clusters, 8 of which are organized as a continuous eT chain connecting FMN and a UQ binding site. One or two UQ-binding sites are located at the interface between the hydrophilic and membrane Complex I domains or in the membrane domain close to the interface area. The hydrophilic domain is composed of 6 or 7 core subunits and protrudes to cytoplasm or mitochondrial matrix. The substrate binding site is located in the open cleft on the surface of the protein. The conserved residues aligning this solvent-accessible cavity form an unusual Rossmann fold, which provides tight packing of the substrate, ensures the planar condensed system of the nicotinamide and the FMN isoalloxazine rings and therefore determines high affinity to NADH, substrate specificity and high rate of hydride transfer to FMN. Structure-function modeling, different mechanistic models, detailed overview | Yarrowia lipolytica |
| physiological function | Complex I catalyzes two-electron NADH oxidation and ubiquinone reduction coupled to the transmembrane translocation of 3 or 4 H+ from negatively charged side (N-side, cytoplasm or mitochondrial matrix) to positively charged side (P-side, periplasm or mitochondrial intermembrane space) of the membrane per 2 electrons | Escherichia coli |
| physiological function | Complex I catalyzes two-electron NADH oxidation and ubiquinone reduction coupled to the transmembrane translocation of 3 or 4H+ from negatively charged side (N-side, cytoplasm or mitochondrial matrix) to positively charged side (P-side, periplasm or mitochondrial intermembrane space) of the membrane per 2 electrons | Thermus thermophilus |
| physiological function | Complex I catalyzes two-electron NADH oxidation and ubiquinone reduction coupled to the transmembrane translocation of 3 or 4H+ from negatively charged side (N-side, cytoplasm or mitochondrial matrix) to positively charged side (P-side, periplasm or mitochondrial intermembrane space) of the membrane per 2 electrons | Yarrowia lipolytica |
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Release 2023.1 (January 2023)
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