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Literature summary extracted from

  • Verkhovskaya, M.; Bloch, D.A.
    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.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.2 membrane
-
 Escherichia coli 16020
-
7.1.1.2 membrane
-
 Thermus thermophilus 16020
-
7.1.1.2 mitochondrial inner membrane
-
 Yarrowia lipolytica 5743
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.2 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
7.1.1.2 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
7.1.1.2 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.1.2 NADH + ubiquinone + 6 H+[side 1] Yarrowia lipolytica
-
 NAD+ + ubiquinol + 7 H+[side 2]
-
 ?
7.1.1.2 NADH + ubiquinone + 6 H+[side 1] Escherichia coli
-
 NAD+ + ubiquinol + 7 H+[side 2]
-
 ?
7.1.1.2 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

EC Number Organism UniProt Comment Textmining
7.1.1.2 Escherichia coli
-
-
-
7.1.1.2 Thermus thermophilus
-
-
-
7.1.1.2 Yarrowia lipolytica
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.2 NADH + ubiquinone + 6 H+[side 1]
-
 Yarrowia lipolytica NAD+ + ubiquinol + 7 H+[side 2]
-
 ?
7.1.1.2 NADH + ubiquinone + 6 H+[side 1]
-
 Escherichia coli NAD+ + ubiquinol + 7 H+[side 2]
-
 ?
7.1.1.2 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]
-
 ?
7.1.1.2 NADH + ubiquinone + 6 H+[side 1]
-
 Thermus thermophilus NAD+ + ubiquinol + 7 H+[side 2]
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.1.2 additional information 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
7.1.1.2 additional information 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
7.1.1.2 additional information 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

Synonyms

EC Number Synonyms Comment Organism
7.1.1.2 complex I
-
 Yarrowia lipolytica
7.1.1.2 complex I
-
 Escherichia coli
7.1.1.2 complex I
-
 Thermus thermophilus
7.1.1.2 NADH:ubiquinone oxidoreductase
-
 Yarrowia lipolytica
7.1.1.2 NADH:ubiquinone oxidoreductase
-
 Escherichia coli
7.1.1.2 NADH:ubiquinone oxidoreductase
-
 Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.2 FMN noncovalently bound Yarrowia lipolytica
7.1.1.2 FMN noncovalently bound Escherichia coli
7.1.1.2 FMN noncovalently bound Thermus thermophilus
7.1.1.2 NADH
-
 Yarrowia lipolytica
7.1.1.2 NADH
-
 Escherichia coli
7.1.1.2 NADH
-
 Thermus thermophilus

General Information

EC Number General Information Comment Organism
7.1.1.2 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
7.1.1.2 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
7.1.1.2 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
7.1.1.2 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
7.1.1.2 additional information potential energy profile for the Complex I substrates and cofactors, overview Escherichia coli
7.1.1.2 additional information potential energy profile for the Complex I substrates and cofactors, overview Thermus thermophilus
7.1.1.2 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
7.1.1.2 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
7.1.1.2 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