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Enzyme Nomenclature
Information on EC 1.6.5.3 - NADH:ubiquinone reductase (H+-translocating)
for references in articles please use BRENDA:EC1.6.5.3
Word Map on EC 1.6.5.3
- 1.6.5.3
- dysfunction
- rotenone
- parkinsonism
- superoxide
-
dopaminergic
- succinate
- neurodegenerative
-
mtdna
-
iron-sulfur
- nigra
-
substantia
-
neuroprotective
- dopamine
-
submitochondrial
-
neurotoxicity
-
bioenergetics
- mpp+
-
rotenone-induced
- epr
- fmn
-
neurotoxin
- leigh
-
subcomplexes
-
oxphos
- 1-methyl-4-phenylpyridinium
- 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
- paracoccus
- leber
- antimycin
-
nadh-cytochrome
- denitrificans
-
nigrostriatal
-
nuclear-encoded
- yarrowia
- alginolyticus
-
homoplasmic
- semiquinone
-
mpp+-induced
-
cybrids
- melas
-
supercomplexes
-
heteroplasmic
-
stroke-like
-
l-shaped
- encephalomyopathy
- ubiquinol
-
ubiquinol-cytochrome
- medicine
- drug development
- degradation
- myxothiazole
- analysis
-
haplogroups
-
mtdna-encoded
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Specify your search results
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.6.5.3
-
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RECOMMENDED NAME
GeneOntology No.
NADH:ubiquinone reductase (H+-translocating)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADH + ubiquinone + 6 H+[side 1] = NAD+ + ubiquinol + 7 H+[side 2]
ping-pong mechanism
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NADH + ubiquinone + 6 H+[side 1] = NAD+ + ubiquinol + 7 H+[side 2]
ping-pong mechanism
-
NADH + ubiquinone + 6 H+[side 1] = NAD+ + ubiquinol + 7 H+[side 2]
reaction mechanism, overview
-
NADH + ubiquinone + 6 H+[side 1] = NAD+ + ubiquinol + 7 H+[side 2]
tri-bi enzyme mechanism combined with a simple model of the conformational changes associated with proton transport, hybrid ping-pong rapid-equilibrium random bi-bi catalytic mechanism, kinetic mechanism and general kinetic model for conformational change in a tri-bi enzyme mechanism, overview
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NADH + ubiquinone + 6 H+[side 1] = NAD+ + ubiquinol + 7 H+[side 2]
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
redox reaction
-
-
-
-
redox reaction
-
the enzyme oxidizes NADH, produced predominantly by the tricarboxylic acid cycle in the mitochondrial matrix, and reduces ubiquinone in the inner mitochondrial membrane
redox reaction
-
no indication for primary or secondary Na+ translocation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
NADH:ubiquinone oxidoreductase
A flavoprotein (FMN) containing iron-sulfur clusters. The complex is present in mitochondria and aerobic bacteria. Breakdown of the complex can release EC 1.6.99.3, NADH dehydrogenase. In photosynthetic bacteria, reversed electron transport through this enzyme can reduce NAD+ to NADH.
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CAS REGISTRY NUMBER
COMMENTARY
9028-04-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mutant derivative of strain BW25113 from which the nuo operon is deleted by genomic replacement
-
-
-
-
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T1KH75 i.e. 49 kDa subunit, A0A1D8X822 i.e. PSST subunit
T1KH75 and A0A1D8X822
UniProt
-
391082, 392676, 392677, 392684, 392699, 392703, 392717, 392718, 392721, 658135, 658174, 658265, 659106, 659108, 659109, 671827, 671882, 671993, 672013, 672126, 672129, 672176, 672291, 672348, 672597, 674495, 674694, 675345, 676868, 696270, 696288, 696312, 696510, 696745, 711290, 714281, 714993, 724383, 724564, 725002, 725003, 725491, 741606, 743263
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-
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392718, 392831, 394359, 659331, 671940, 672008, 672041, 672043, 672349, 673614, 673620, 673940, 674624, 675494, 690948, 696147, 696380, 696387, 698799, 725142, 725443, 725517, 741891, 742759, 742808
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-
mutant derivative of strain BW25113 from which the nuo operon is deleted by genomic replacement
-
-
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392697, 671733, 672974, 673615, 675345, 690713, 691039, 691049, 692447, 692992, 693815, 694192, 694352, 694936, 695189, 696382, 696388, 697166, 698312, 699152, 726174, 743265
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
-
the complex I subunits NuoL, NuoM and NuoN are homologous to two proteins, MrpA and MrpD, from one particular class of Na+/H+ antiporters. In many bacteria MrpA and MrpD are encoded by an operon comprising 6-7 conserved genes
evolution
-
complex I has been subject to a phenomenal increase in size that predates the diversification of extant eukaryotes, followed by very few lineage-specific additions/losses of subunits
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
evolution
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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
evolution
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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
malfunction
-
electron transfer and proton translocation activity of complex I variants lacking either NuoL or parts of the C-terminal domain, overview
malfunction
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deletion of either mrpA or mrpD from the Bacillus subtilis chromosome resulted in a Na+ and pH sensitive growth phenotype. NuoL can rescue Bacillus subtilis DELTAmrpA, but improved the growth of Bacillus subtilis DELTAmrpD only slightly. NuoN can restore the wild type properties of Bacillus subtilis DELTAmrpD, but has no effect on the ?mrpA strain. Expression of NuoM does not result in any growth improvement under these conditions. This reveals that the complex I subunits NuoL, NuoM and NuoN also demonstrate functional specializations
malfunction
Chlamydomonas sp.
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when present in the homoplasmic state in the alga, the mutation does not prevent assembly of the whole complex I, the NADH dehydrogenase activity of the peripheral arm of the complex is mildly affected. The NADH:duroquinone oxidoreductase activity is strongly reduced, suggesting that the substitution could affect binding of ubiquinone to the membrane domain. The membrane potential is not affected in mutant mitochondria. The in vitro defects correlate with a decrease in dark respiration and growth rate in vivo, phenotype, overview
malfunction
-
defects in complex I are the most frequent cause of human respiratory disorders. Substitution L158P does not lead to any respiratory enzyme defects when present in the heteroplasmic state in a patient with chronic progressive external ophthalmoplegia
malfunction
-
electron transfer and proton translocation activity of complex I variants lacking either NuoL or parts of the C-terminal domain, overview
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physiological function
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involved in aromatic amino acid metabolism
physiological function
Vitis vinifera x Vitis vinifera
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involved in aromatic amino acid metabolism
physiological function
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the NuoG subunit of the type I NADH dehydrogenase, NDH-1, is important in Mycobacterium tuberculosis-mediated inhibition of host macrophage apoptosis, the NDH-1 complex is important for NOX2 neutralization in host macrophages
physiological function
-
NDE2 is the main external dehydrogenase responsible for the oxidation of cytosolic NADH and NADPH under physiological conditions
physiological function
-
Ndi1p functionally interacts with the nematode respiratory chain and contributes to the formation of the mitochondrial membrane potential in vivo. Ndi1p expression results in significantly improved reproductive success, better survival under conditions of oxidative stress, fewer signs of premature aging, increased respiration rates and a complete restoration of the in vivo mitochondrial membrane potential in Caenorhabditis elegans nuo-1 mutants. However, Ndi1p is not able to fully replace complex I and cannot support larval development when complex I is missing
physiological function
-
respiratory complex I couples the transfer of electrons from NADH to ubiquinone with a translocation of protons across the membrane
physiological function
-
NADH:ubiquinone oxidoreductase (complex I) is a complicated respiratory enzyme that conserves the energy from NADH oxidation, coupled to ubiquinone reduction, as a proton motive force across the mitochondrial inner membrane. During catalysis, NADH oxidation by a flavin mononucleotide is followed by electron transfer to a chain of iron-sulfur clusters. Alternatively, the flavin may be reoxidized by hydrophilic electron acceptors, by artificial electron acceptors in kinetic studies, or by oxygen and redox-cycling molecules to produce reactive oxygen species
physiological function
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MrpA transports Na+ whereas MrpD transports H+ in opposite directions, resulting in antiporter activity, besides one Na+ channel, NuoL, and two H+ channels, NuoM and NuoN, are present.
physiological function
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complex I is one of the respiratory complexes that generate the proton-motive force required for the synthesis of ATP in mitochondria. The electron transfer from NADH to ubiquinone through protein-bound prosthetic groups, which is coupled to the translocation of protons across the inner mitochondrial membrane
physiological function
-
the flavin mononucleotide in complex I catalyzes NADH oxidation, O2 reduction to superoxide, and the reduction of several artificial electron acceptors
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
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
physiological function
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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
physiological function
-
the respiratory complex I couples the electron transfer from NADH to ubiquinone with a translocation of protons across the membrane
physiological function
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in mitochondria, complex I (NADH:ubiquinone oxidoreductase) uses the redox potential energy from NADH oxidation by ubiquinone to transport protons across the inner membrane, contributing to the proton-motive force
physiological function
-
NADH:ubiquinone oxidoreductase (complex I) pumps protons across the membrane using downhill redox energy
physiological function
The enzyme's major function is the transfer of two electrons from NADH (matrix side) to ubiquinone (inner mitochondrial membrane), biochemical function and physiological role of diverse plant specific complex I subunits, overview
physiological function
protein NrcN functions independently of other components of the putative Nrc complex
physiological function
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subunit NuoL is involved in the high efficiency pumping mechanism in complex I
physiological function
-
complex I is invovled in in lipopolysaccharide action in macrophages
physiological function
after reconstituting isolated AIFM1 into bacterial or mitochondrial membranes, N-terminally tagged AIFM1 displays substantial NADH:O2 activity and supports NADH-linked proton pumping activities in the host membranes. Overexpressing N-terminally tagged AIFM1 and AIF-homologous mitochondrion-associated inducer of death AMID enhances the growth of a double knock-out Escherichia coli strain lacking complex I and NDH-2. C-terminally tagged AIFM1 and NADH-binding site mutants of N-terminally tagged AIFM1 and AMID fail to show both NADH:O2 activity and the growth-enhancing effect; after reconstituting isolated AIFM2 into bacterial or mitochondrial membranes, N-terminally tagged AIFM2 displays substantial NADH:O2 activity and supports NADH-linked proton pumping activities in the host membranes. Overexpressing N-terminally tagged AIFM1 and AIFM2 enhances the growth of a double knock-out Escherichia coli strain lacking complex I and NDH-2. NADH-binding site mutants of N-terminally tagged AIFM1 and AIFM2 fail to show both NADH:O2 activity and the growth-enhancing effect
physiological function
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inducible knockdown of NDH2 has a modest growth effect in bloodstream forms, but NDH2 null mutants, as well as inducible knockdowns in a complex I deficient back-ground, show a greater reduction in growth. Loss of NDH2 leads to reduced levels of acetate, which is required for several essential pathways in bloodstream form Trypanosoma brucei
physiological function
improper splicing of Nad1 transcripts leads to the absence of mitochondrial complex I and alteration of the nuclear transcriptome
physiological function
rerouting electrons through the NDA2 catalytic hub in response to photoautotrophic N deprivation sustains cell viability while promoting the dissipation of excess excitation energy through quenching and chlororespiratory processes. The type II NADPH dehydrogenase is key to acclimation of cells to N deprivation. NDA2 drives cyclic electron flow, chlororespiration, and the generation of an H+ gradient across the thylakoid membranes. N deprivation elicits a doubling of the rate of NDA2-dependent cyclic electron flow, with little contribution from PGR5/PGRL1-dependent cyclic electron flow. Stimulation of NDA2-dependent chlororespiration affords additional relief from the elevated reduction state associated with N deprivation through plastid terminal oxidase-dependent water synthesis
physiological function
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improper splicing of Nad1 transcripts leads to the absence of mitochondrial complex I and alteration of the nuclear transcriptome
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physiological function
-
Ndi1p functionally interacts with the nematode respiratory chain and contributes to the formation of the mitochondrial membrane potential in vivo. Ndi1p expression results in significantly improved reproductive success, better survival under conditions of oxidative stress, fewer signs of premature aging, increased respiration rates and a complete restoration of the in vivo mitochondrial membrane potential in Caenorhabditis elegans nuo-1 mutants. However, Ndi1p is not able to fully replace complex I and cannot support larval development when complex I is missing
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physiological function
-
respiratory complex I couples the transfer of electrons from NADH to ubiquinone with a translocation of protons across the membrane
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physiological function
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the NuoG subunit of the type I NADH dehydrogenase, NDH-1, is important in Mycobacterium tuberculosis-mediated inhibition of host macrophage apoptosis, the NDH-1 complex is important for NOX2 neutralization in host macrophages
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physiological function
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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protein NrcN functions independently of other components of the putative Nrc complex
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additional information
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the complex consists of a peripheral arm catalyzing the electron transfer reaction and a membrane arm involved in proton translocation. The energy released by the redox reaction is transmitted to the membrane arm via a conformational change in the horizontal helix. The helix corresponds to the C-terminal part of the most distal subunit NuoL. The C-terminal domain of NuoL is essential for the translocation of 2H+/2e-
additional information
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mechanism of NADH oxidation by complex I, the adenosine moiety of NADH is crucial for binding, overview
additional information
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the accessory’ subunits of eukaryotic complex I bear an allosteric ATP binding site
additional information
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the accessory subunits of eukaryotic complex I bear an allosteric ATP binding site
additional information
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the accessory subunits of eukaryotic complex I bear an allosteric ATP binding site
additional information
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NuoA is a small membrane spanning subunit of respiratory chain NADH:quinone oxidoreductase (complex I). Unlike the other complex I core protein subunits, the NuoA protein has no known homologue in other enzyme systems
additional information
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potential energy profile for the Complex I substrates and cofactors, overview
additional information
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potential energy profile for the Complex I substrates and cofactors, overview
additional information
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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
additional information
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the deactive state of complex I is formed during hypoxia, when respiratory chain turnover is slowed, and may contribute to determining the outcome of ischemia-reperfusion injury
additional information
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the complex consists of a peripheral arm catalyzing the electron transfer reaction and a membrane arm involved in proton translocation. The energy released by the redox reaction is transmitted to the membrane arm via a conformational change in the horizontal helix. The helix corresponds to the C-terminal part of the most distal subunit NuoL. The C-terminal domain of NuoL is essential for the translocation of 2H+/2e-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-dimethyl-1,4-naphthoquinone + NADH + H+
2,3-dimethyl-1,4-hydronaphthoquinol + NAD+
-
-
-
-
?
amplex red + NADH + O2
resorufin + NAD+ + H2O2
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the rate of H2O2 formation by complex I strongly depends upon the NAD+/NADH ratio
-
-
?
deamino-NADH + dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
deamino-NAD+ + reduced dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
-
-
-
?
deamino-nicotinamide-adeninedinucleotide + n-decylubiquinone
? + n-decylubiquinol
-
-
-
-
?
dihydroethidium + O2
ethidium + H2O2
-
dihydroethidium reduction shows that, upon reducing O2, it produces approximately 20% superoxide and 80% H2O2
-
-
?
NADH + 1,1'-carbamoylmethylviologen
NAD+ + reduced 1,1'-carbamoylmethylviologen
-
-
-
-
r
NADH + 2,3-dimethoxy-5-methyl-6-[(6-methyl-2,3-dihydroimidazo[2,1-b][1,3]thiazol-5-yl)methyl]benzo-1,4-quinone
NAD+ + ?
NADH + 2,3-dimethoxy-5-methyl-6-[(6-methylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]benzo-1,4-quinone
NAD+ + ?
-
-
-
-
?
NADH + 2,3-dimethoxy-5-methyl-6-[(6-phenylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]benzo-1,4-quinone
NAD+ + ?
-
-
-
-
?
NADH + 2-methyl-1,4-naphthoquinone
NAD+ + 2-methyl-1,4-naphthoquinol
-
-
-
-
?
NADH + 2-[(2,6-dimethylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
NAD+ + ?
-
-
-
-
?
NADH + 2-[(2-chloro-6-methylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
NAD+ + ?
-
-
-
-
?
NADH + 2-[(2-chloro-6-phenylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
NAD+ + ?
-
-
-
-
?
NADH + 2-[(6-chloro-2,3-dihydroimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
NAD+ + ?
-
-
-
-
?
NADH + 2-[(6-chloro-2-methylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
NAD+ + ?
-
-
-
-
?
NADH + 2-[(6-chloroimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
NAD+ + ?
-
-
-
-
?
NADH + H+ + 2,5-dimethyl-1,4-benzoquinone
NAD+ + 2,5-dimethyl-1,4-benzoquinol
-
-
-
-
?
NADH + H+ + 2-methyl-1,4-naphthoquinone
NAD+ + 2-methyl-1,4-naphthoquinol
-
-
-
-
?
NADH + H+ + 5,8-dioxo-1,4-naphthoquinone
NAD+ + 5,8-dioxo-1,4-naphthoquinol
-
-
-
-
?
NADH + H+ + idebenone
NAD+ + ?
-
studies of ubiquinone reduction by isolated complex I are problematic because the extremely hydrophobic natural substrate, ubiquinone-10, must be substituted with a relatively hydrophilic analogue (such as ubiquinone-1). Hydrophilic ubiquinones are reduced by an additional, non-energy-transducing pathway. Inhibitor-insensitive ubiquinone reduction occurs by a ping-pong type mechanism, catalyzed by the flavin mononucleotide cofactor in the active site for NADH oxidation. Moreover, semiquinones produced at the flavin site initiate redox cycling reactions with molecular oxygen, producing superoxide radicals and hydrogen peroxide. The ubiquinone reactant is regenerated, so the NADH:Q reaction becomes superstoichiometric. Idebenone, an artificial ubiquinone, reacts at the flavin site
-
-
?
NADH + H+ + menaquinone
NAD+ + menaquinol
-
the enzyme plays an essential role in maintaining a reduced ubiquinone-pool during infection (Mycobacterium tuberculosis is the causative agents of tuberculosis). The enzyme is not only essential to parasite survival in vivo but may also contribute to the severity and outcome of disease. Type II NADH:quinone oxidoreductase the membrane-bound respiratory enzyme differs from the canonical NADH:dehydrogenase (complex I), because it is not involved in the vectorial transfer of protons across membranes. Mycobacterium tuberculosis contains a branched respiratory chain terminating in a cytochrome bd (quinol) oxidase and an aa3-type cytochrome c oxidase. Both chains are fed by a menaquinol (MQH2) pool that is generated by four dehydrogenases; one succinate menaquinone oxidoreductase (SQR), one multimeric type I NADH: dehydrogenase (complex I), and two type II NADH: menaquinone oxidoreductases (ndh and ndhA). Transposon insertion knockout strategy reveals that disruption of the ndh gene is lethal
-
-
?
NADH + H+ + oxidized dichlorophenolindophenol
NAD+ + reduced dichlorophenolindophenol
-
-
-
-
?
NADH + H+ + tetramethyl-1,4-benzoquinone
NAD+ + tetramethyl-1,4-benzoquinol
-
-
-
-
?
NADH + nitroblue tetrazolium
NAD+ + reduced nitroblue tetrazolium
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
NADH + oxidized coenzyme Q1 + 5 H+[side1]
NAD+ + reduced coenzyme Q1 + 4 H+[side2]
-
-
-
?
NADH + oxidized coenzyme Q1 + 5 H+[side1]
NAD+ + reduced coenzyme Q1 + 4H+[side2]
-
-
-
?
NADPH + 2-methylnaphthoquinone
NADP+ + ?
-
about 1% of the activity with NADH
-
-
?
NADPH + ubiquinone + 6 H+[side 1]
NADP+ + ubiquinol + 7 H+[side 2]
-
NADPH is a poor substrate of the complex
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
?
2 ferricyanide + deamino-NADH
2 ferrocyanide + deamino-NAD+ + H+
-
-
-
-
?
2 ferricyanide + deamino-NADH
2 ferrocyanide + deamino-NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
232.7% of the activity with ubiquinone-1
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
activity is 27.4fold of the activity with ubiquinone-1
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
0.13% of the activity with NADH and ferricyanide
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
about 1% of the activity with NADH
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
8.3% of the activity with ubiquinone-1
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
12%-16% of the activity with ubiquinone-1
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2-methyl-1,4-naphthoquinone + NADH + H+
2-methyl-1,4-naphthoquinol + NAD+
-
specific for NADH
-
-
?
2-methyl-1,4-naphthoquinone + NADH + H+
2-methyl-1,4-naphthoquinol + NAD+
-
i.e. menadione
-
-
?
NADH + 2,3-dimethoxy-5-methyl-6-[(6-methyl-2,3-dihydroimidazo[2,1-b][1,3]thiazol-5-yl)methyl]benzo-1,4-quinone
NAD+ + ?
-
-
-
-
?
NADH + 2,3-dimethoxy-5-methyl-6-[(6-methyl-2,3-dihydroimidazo[2,1-b][1,3]thiazol-5-yl)methyl]benzo-1,4-quinone
NAD+ + ?
-
-
-
-
?
NADH + 2-methylnaphthoquinone
NAD+ + ?
-
7.6% of the activity with ubiquinone-1
-
-
?
NADH + decylubiquinone
NAD+ + decylubiquinol
-
-
-
-
?
NADH + decylubiquinone
NAD+ + decylubiquinol
-
no activity with the enzymatically active subcomplexes Ilambda, IS, and IlamdaS at similar rates to complex I
-
-
?
NADH + decylubiquinone
NAD+ + decylubiquinol
-
ordered sequential mechanism in which the order of substrate bindings and product release is: NADH, decylubiquinone, decylubiquinol, NAD+
-
-
?
NADH + duroquinone
NAD+ + duroquinol
-
64.5% of the activity with ubiquinone-1
-
-
?
NADH + H+ + coenzyme Q1
NAD+ + reduced coenzyme Q1
-
ordered sequential mechanism in which the order of substrate binding and product release is coenzyme Q1, NADH, NAD+ and reduced coenzyme coenzyme Q1
-
-
?
NADH + H+ + decylubiquinone
NAD+ + decylubiquinol
-
decylubiquinone is slightly better than ubiquinone-1 as electron acceptor
-
-
?
NADH + H+ + decylubiquinone
NAD+ + decylubiquinol
-
the enzyme is selective for NADH
-
-
?
NADH + H+ + decylubiquinone
NAD+ + decylubiquinol
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
NADH + H+ + duroquinone
NAD+ + duroquinol
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
the energy-converting NADH:ubiquinone oxidoreductase (respiratory complex I), couples the transfer of electrons from NADH to ubiquinone with the translocation of protons across the membrane
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
NADH:ubiquinone oxidoreductase or complex I is a large multisubunit assembly of the mitochondrial inner membrane that channels high-energy electrons from metabolic NADH into the electron transport chain. Its dysfunction is associated with a range of progressive neurological disorders, often characterized by a very early onset and short devastating course. Reduction in cellular complex I activity leads to a depolarization of the mitochondrial membrane potential, resulting in a decreased supply of mitochondrial ATP to the Ca2+-ATPases of the intracellular stores and thus to a reduced Ca2+ content of these stores
-
-
?
NADH + H+ + ubiquinone-0
NAD+ + ubiquinol-0
-
prefers ubiquinol-0 as an acceptor substrate, and can also use the artificial electron acceptors, menadione and dichlorophenol–indophenol
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
-
formation of the semiquinone signals during steady state electron transfer from NADH to ubiquinone-1
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
-
studies of ubiquinone reduction by isolated complex I are problematic because the extremely hydrophobic natural substrate, ubiquinone-10, must be substituted with a relatively hydrophilic analogue (such as ubiquinone-1). Hydrophilic ubiquinones are reduced by an additional, non-energy-transducing pathway. Inhibitor-insensitive ubiquinone reduction occurs by a ping-pong type mechanism, catalyzed by the flavin mononucleotide cofactor in the active site for NADH oxidation. Moreover, semiquinones produced at the flavin site initiate redox cycling reactions with molecular oxygen, producing superoxide radicals and hydrogen peroxide. The ubiquinone reactant is regenerated, so the NADH:Q reaction becomes superstoichiometric. Idebenone, an artificial ubiquinone, reacts at the flavin site
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
NADH + H+ + ubiquinone-10
NAD+ + ubiquinol-10
-
the natural substrate ubiquinone-10 is extremely hydrophobic
-
-
?
NADH + H+ + ubiquinone-10
NAD+ + ubiquinol-10
-
studies of ubiquinone reduction by isolated complex I are problematic because the extremely hydrophobic natural substrate, ubiquinone-10, must be substituted with a relatively hydrophilic analogue (such as ubiquinone-1). Hydrophilic ubiquinones are reduced by an additional, non-energy-transducing pathway. Inhibitor-insensitive ubiquinone reduction occurs by a ping-pong type mechanism, catalyzed by the flavin mononucleotide cofactor in the active site for NADH oxidation. Moreover, semiquinones produced at the flavin site initiate redox cycling reactions with molecular oxygen, producing superoxide radicals and hydrogen peroxide. The ubiquinone reactant is regenerated, so the NADH:Q reaction becomes superstoichiometric. Idebenone, an artificial ubiquinone, reacts at the flavin site
-
-
?
NADH + H+ + vitamin K2
NAD+ + reduced vitamin K2
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
NADH + H+ + vitamin K2
NAD+ + vitamin K2
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
NADH + menadione
NAD+ + menadiol
-
menadione is a poor electron acceptor
-
?
NADH + n-decylubiquinone + 5 H+[side1]
NAD+ + n-decylubiquinol + 4H+[side2]
-
-
-
?
NADH + n-decylubiquinone + 5 H+[side1]
NAD+ + n-decylubiquinol + 4H+[side2]
-
-
-
?
NADH + n-decylubiquinone + H+
NAD+ + n-decylubiquinol
-
-
-
-
?
NADH + O2
NAD+ + superoxide radical
-
addition of NADH, but not decylubiquinol, leads to superoxide production
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
41.7% of the activity with ubiquinone-1
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
2,6-dichlorophenolindophenol is a poor electron acceptor
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
2,6-dichlorophenol indophenol as electron acceptor
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
-
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + ubiquinone
?
-
NADH-ubiquinone reductase complex I is involved in the respiratory chain
-
-
?
NADH + ubiquinone
?
-
vectorial electron translocation is coupled to electron transfer
-
-
-
NADH + ubiquinone
?
-
mutations in NADH:ubiquinone oxidoreductase NADH of Escherichia coli affect growth on mixed amino acids, because the large NADH/NAD+ ratio inhibits enzymes, e.g. citrate synthase and malate dehydrogenase, shared by the tricarboxylic acid cycle and the glyoxylate shunt
-
-
?
NADH + ubiquinone
?
-
the enzyme catalyzes the transfer of electrons without translocation of protons across the membrane
-
-
-
NADH + ubiquinone
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
proton-translocating enzyme
-
-
?
NADH + ubiquinone
?
-
proton-translocating NADH-ubiquinone oxidoreductase is the largest multiprotein complex of the respiratory chain
-
-
?
NADH + ubiquinone
NAD+ + ubiquinol
-
-
391082, 392676, 392677, 392684, 392691, 392699, 392703, 392717, 392718, 392721, 671827, 671993, 672129, 672176, 672291, 672348, 672597, 675345, 676868
-
-
?
NADH + ubiquinone
NAD+ + ubiquinol
-
-
-
-
?
NADH + ubiquinone
NAD+ + ubiquinol
-
-
-
-
?
NADH + ubiquinone
NAD+ + ubiquinol
-
proton-translocating enzyme
-
-
?
NADH + ubiquinone
NAD+ + ubiquinol
-
-
-
-
?
NADH + ubiquinone
NAD+ + ubiquinol
-
proton-translocating enzyme
-
-
?
NADH + ubiquinone
NAD+ + ubiquinol
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
proton-translocating enzyme
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
-
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
-
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
-
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
-
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
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)
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
-
-
-
?
NADH + ubiquinone-1
NAD+ + ubiquinol-1
-
reaction is catalyzed by the enzymatically active subcomplexes Ilambda, IS, and IlamdaS at similar rates to complex I
-
-
?
NADH + ubiquinone-1 + 5 H+[side 1]
NAD+ + ubiquinol-1 + 4 H+[side 2]
-
-
-
-
?
NADH + ubiquinone-1 + 5 H+[side 1]
NAD+ + ubiquinol-1 + 4 H+[side 2]
-
-
-
-
?
NADH + ubiquinone-1 + 5 H+[side 1]
NAD+ + ubiquinol-1 + 4 H+[side 2]
-
-
-
?
NADH + ubiquinone-6
NAD+ + ubiquinol-6
-
86% of the activity with ubiquinone-1
-
-
?
NADPH + H+ + ubiquinone
NADP+ + ubiquinol
-
the enzyme has a lower affinity to NADPH than to NADH
-
-
?
NADPH + H+ + ubiquinone
NADP+ + ubiquinol
Agrobacterium tumefaciens C58 / ATCC 33970
-
the enzyme has a lower affinity to NADPH than to NADH
-
-
?
ubiquinone-1 + NADH + H+
ubiquinol-1 + NAD+
-
the protein shows NADH-ubiquinone-1 oxidoreductase activity, NADPH oxidase (EC 1.6.3.1) and NADPH-ubiquinone-1 oxidoreductase (EC 1.6.5.2) activities
-
-
?
additional information
?
-
-
NADH-NADP transhydrogenation at a very slow rate
-
-
-
additional information
?
-
-
no redox-coupled Na+ transport, but the deactive form of complex I, which is formed spontaneously when enzyme turnover is precluded by lack of substrates, is a Na+/H+ antiporter. The antiporter activity is Na+-specific and is abolished upon reactivation by the addition of substrates and by the complex I inhibitor rotenone. It is specific for Na+ over K+
-
-
-
additional information
?
-
-
the enzyme shows also rotenone-insensitive NADH:hexaammineruthenium III (HAR) oxidoreductase activity
-
-
-
additional information
?
-
-
the positively-charged electron acceptors paraquat and hexaammineruthenium(III) react with the nucleotide-bound reduced flavin in complex I, by an unusual ternary mechanism, overview. The mechanism for paraquat reduction defines another mechanism for superoxide production by complex I by redox cycling
-
-
-
additional information
?
-
-
complex I is a primary electrogenic proton pump and may be capable of secondary sodium antiport. The magnitude of the pH-gradient depends on the sodium concentration
-
-
-
additional information
?
-
-
FMN-dependent NADH-quinone reductase induced by menadione
-
-
-
additional information
?
-
-
midpoint potentials for the redox transitions of the quinone radicals in complex I are -37 and -235 mV at pH 6 with an absorption around 325 nm and a fluorescence emission at 460/475 nm
-
-
-
additional information
?
-
-
NADH:ubiquinone oxidoreductase (EC 1.6.5.3) constitutes the entry point of electrons in the electron transport chain. Mitochondrial NADH:ubiquinone oxidoreductase or complex I (CI) is a frequently affected enzyme in cases of mitochondrial disorders
-
-
-
additional information
?
-
-
computational model of mammalian complex I for catalysis. The fully reduced FMN and semiquinone are the primary sources of superoxide, and the iron-sulfur cluster N2 produces none. The FMN radical only produces reactive oxygen species when the quinone reductase site is blocked. Reaxtive oxygen species generation is maximized during reverse electron transport with both the FMN and semiquinone producing similar amounts of superoxide. The model successfully predicts the increase in reactive oxygen species generation when the membrane potential is high and matrix pH is alkaline
-
-
-
additional information
?
-
-
the enzyme mediates electron transfer to particulate methane monooxygenase
-
-
-
additional information
?
-
-
does not react with NADPH or oxygen
-
-
-
additional information
?
-
-
enzyme catalyzes the transfer electrons from NADH to quinone substrates by a nonclassical, two-site pingpong kinetic mechanism whereby substrate quinones bind to a site that is distinct from the NADH-binding site. Presence of two binding sites for quinone ligands, one favoring the reduced form and the other favoring the oxidized form
-
-
-
additional information
?
-
-
the enzyme shows also rotenone-insensitive NADH:hexaammineruthenium III (HAR) oxidoreductase activity. The enzyme NDH-1 catalyzes a number of the NADH:artificial electron acceptor oxidoreductase activities showing particularly high turnover numbers with ferricyanide and hexaammineruthenium(III), kinetic patterns of the steady-state NADH oxidation with these two electron acceptors, overview
-
-
-
additional information
?
-
-
no activity with coenzyme Q4 and coenzyme QD
-
-
-
additional information
?
-
-
superoxide production from complex I is large under conditions of reverse electron transport. Production of superoxide by complex I during reverse electron transport is at least 3fold more sensitive to the pH gradient than to the membrane potential
-
-
-
additional information
?
-
-
superoxide production rates by complex I during reverse electron transfer are much greater than during forwards electron transfer. The major site of superoxide production in complex I is the quinpone-binding site, it is most likely a semiquinone
-
-
-
additional information
?
-
-
hexaammineruthenium (III) chloride, i.e. HAR, can act as artificial electron acceptor. The rate of NADH oxidation by the artificial electron acceptor HAR is about 10fold higher than NADH oxidase activity and is insensitive to rotenone and piericidin
-
-
-
additional information
?
-
-
no redox-coupled Na+ transport and no Na+/H+ antiporter function by the enzyme from Yarrowia lipolytica
-
-
-
additional information
?
-
-
the enzyme shows also rotenone-insensitive NADH:hexaammineruthenium III (HAR) oxidoreductase activity
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADH + H+ + menaquinone
NAD+ + menaquinol
-
the enzyme plays an essential role in maintaining a reduced ubiquinone-pool during infection (Mycobacterium tuberculosis is the causative agents of tuberculosis). The enzyme is not only essential to parasite survival in vivo but may also contribute to the severity and outcome of disease. Type II NADH:quinone oxidoreductase the membrane-bound respiratory enzyme differs from the canonical NADH:dehydrogenase (complex I), because it is not involved in the vectorial transfer of protons across membranes. Mycobacterium tuberculosis contains a branched respiratory chain terminating in a cytochrome bd (quinol) oxidase and an aa3-type cytochrome c oxidase. Both chains are fed by a menaquinol (MQH2) pool that is generated by four dehydrogenases; one succinate menaquinone oxidoreductase (SQR), one multimeric type I NADH: dehydrogenase (complex I), and two type II NADH: menaquinone oxidoreductases (ndh and ndhA). Transposon insertion knockout strategy reveals that disruption of the ndh gene is lethal
-
-
?
NADH + H+ + ubiquinone-10
NAD+ + ubiquinol-10
-
the natural substrate ubiquinone-10 is extremely hydrophobic
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
the energy-converting NADH:ubiquinone oxidoreductase (respiratory complex I), couples the transfer of electrons from NADH to ubiquinone with the translocation of protons across the membrane
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
NADH:ubiquinone oxidoreductase or complex I is a large multisubunit assembly of the mitochondrial inner membrane that channels high-energy electrons from metabolic NADH into the electron transport chain. Its dysfunction is associated with a range of progressive neurological disorders, often characterized by a very early onset and short devastating course. Reduction in cellular complex I activity leads to a depolarization of the mitochondrial membrane potential, resulting in a decreased supply of mitochondrial ATP to the Ca2+-ATPases of the intracellular stores and thus to a reduced Ca2+ content of these stores
-
-
?
NADH + ubiquinone
?
-
NADH-ubiquinone reductase complex I is involved in the respiratory chain
-
-
?
NADH + ubiquinone
?
-
vectorial electron translocation is coupled to electron transfer
-
-
-
NADH + ubiquinone
?
-
mutations in NADH:ubiquinone oxidoreductase NADH of Escherichia coli affect growth on mixed amino acids, because the large NADH/NAD+ ratio inhibits enzymes, e.g. citrate synthase and malate dehydrogenase, shared by the tricarboxylic acid cycle and the glyoxylate shunt
-
-
?
NADH + ubiquinone
?
-
the enzyme catalyzes the transfer of electrons without translocation of protons across the membrane
-
-
-
NADH + ubiquinone
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
proton-translocating enzyme
-
-
?
NADH + ubiquinone
?
-
proton-translocating NADH-ubiquinone oxidoreductase is the largest multiprotein complex of the respiratory chain
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
-
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
-
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
-
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
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)
-
-
?
NADH + ubiquinone + 6 H+[side 1]
NAD+ + ubiquinol + 7 H+[side 2]
-
-
-
-
?
additional information
?
-
-
no redox-coupled Na+ transport, but the deactive form of complex I, which is formed spontaneously when enzyme turnover is precluded by lack of substrates, is a Na+/H+ antiporter. The antiporter activity is Na+-specific and is abolished upon reactivation by the addition of substrates and by the complex I inhibitor rotenone. It is specific for Na+ over K+
-
-
-
additional information
?
-
-
complex I is a primary electrogenic proton pump and may be capable of secondary sodium antiport. The magnitude of the pH-gradient depends on the sodium concentration
-
-
-
additional information
?
-
-
FMN-dependent NADH-quinone reductase induced by menadione
-
-
-
additional information
?
-
-
NADH:ubiquinone oxidoreductase (EC 1.6.5.3) constitutes the entry point of electrons in the electron transport chain. Mitochondrial NADH:ubiquinone oxidoreductase or complex I (CI) is a frequently affected enzyme in cases of mitochondrial disorders
-
-
-
additional information
?
-
-
the enzyme mediates electron transfer to particulate methane monooxygenase
-
-
-
additional information
?
-
-
superoxide production from complex I is large under conditions of reverse electron transport. Production of superoxide by complex I during reverse electron transport is at least 3fold more sensitive to the pH gradient than to the membrane potential
-
-
-
additional information
?
-
-
superoxide production rates by complex I during reverse electron transfer are much greater than during forwards electron transfer. The major site of superoxide production in complex I is the quinpone-binding site, it is most likely a semiquinone
-
-
-
additional information
?
-
-
no redox-coupled Na+ transport and no Na+/H+ antiporter function by the enzyme from Yarrowia lipolytica
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
riboflavin
complex contains one non-covalently bound FAD, one noncovalently bound riboflavin, ubiquinone-8 and a [2Fe–2S] cluster.. The phosphate group is attached at the 5'-position of the ribityl as in authentic FMN and the NADH:quinone oxidoreductase contains approximately 1.7 mol covalently bound FMN per mol non-covalently bound FAD. Each of the single NqrB and NqrC subunits in the NADH:quinone oxidoreductase carries a single FMN
Ubiquinone-10
-
the enzyme contains 4.2-4.5 mol of ubiquinone-10 per 650000 Da enzyme
ubiquinone-8
complex contains one non-covalently bound FAD, one noncovalently bound riboflavin, ubiquinone-8 and a [2Fe–2S] cluster
[2Fe-2S]-center
complex contains one non-covalently bound FAD, one noncovalently bound riboflavin, ubiquinone-8 and a [2Fe–2S] cluster
FAD
-
requires FMN or FAD as cofactor, FMN is more effective. Half-maximum activity is obtained with 0.00054 mM FMN or 0.0165 mM FAD
FAD
complex contains one non-covalently bound FAD, one noncovalently bound riboflavin, ubiquinone-8 and a [2Fe–2S] cluster. The phosphate group is attached at the 5'-position of the ribityl as in authentic FMN and the NADH:quinone oxidoreductase contains approximately 1.7 mol covalently bound FMN per mol non-covalently bound FAD
FAD
FAD content of homologously produced NrcN is 1 mol of FAD/mol protein. FAD is not covalently bound; UV-Vis spectrum shows a shoulder at 465 nm. FAD is not covalently bound
FMN
-
enzyme requires FMN or FAD as cofactor, FMN is 30times more effective. Half-maximum activity is obtained with 0.00054 mM FMN or 0.0165 mM FAD
FMN
-
covalently attached. The average reduction potential of the FMN is + 160 mV, at 25°C and pH 6.5
FMN
-
contains non-covalently bound flavin mononucleotide. Hydrophilic ubiquinones are reduced by an additional, non-energy-transducing pathway. Inhibitor-insensitive ubiquinone reduction occurs by a ping-pong type mechanism, catalyzed by the flavin mononucleotide cofactor in the active site for NADH oxidation
NADH
-
binding to the enzyme results in a conformational change, in the coenzyme Q binding site, which enables the site to accept coenzyme Q with a side chain significantly larger than one isoprenoid unit
NADH
-
both arms of the Escherichia coli complex I are widened after the addition of NADH but not of NADPH. NADH-induced conformational changes are also detected in solution
NADH
-
the NADH binding site is located in the matrix of mitochondria and their inner membrane is impermeable for NADH
NADH
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the adenosine moiety is crucial for binding, while the nicotinamide is detrimental to binding
NADH
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-
NADH
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binding of NADH includes interactions of the hydroxyl groups of the adenosine ribose with a conserved glutamic acid residue. Structural analysis revealed that due to steric hindrance and electrostatic repulsion, this residue most likely prevents the binding of NADPH, which is a poor substrate of the complex
NADH
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391082, 392676, 392677, 392684, 392691, 392692, 392699, 392703, 392717, 392718, 392721, 658135, 658174, 659106, 659109, 671827, 671882, 671993, 672013, 672126, 672129, 672176, 672291, 672348, 672597, 674495, 674694, 675345, 676868, 696270, 696288, 696312, 696510, 707505, 711290, 714281, 714993, 724564, 725002, 725003, 725491
NADH
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-
392678, 392681, 392682, 392692, 392718, 392831, 659206, 659331, 671940, 672008, 672041, 672043, 672349, 673614, 673620, 673940, 674624, 675494, 696380, 724310, 725142, 725517
NADPH
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addition of NADH but not NADPH leads to an extension of the overall structure of the complex, although all cofactors of the complex are reduced by NADPH
additional information
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the enzyme contains only substoichiometric amounts of ubiquinone-9, 0.2-0.4 mol/mol
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additional information
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[2Fe-2S] cluster N1a is not the reductant of O2 in complex I, but has a specific role in determining the outcome of O2 reduction
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additional information
no cofactor: deamino-NADH; no cofactor: deamino-NADH
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additional information
no cofactor: deamino-NADH; no cofactor: deamino-NADH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe-S
Fe2+
Iron
Mg2+
[4Fe-4S] center
Fe
-
contains eight iron-sulfur clusters. Seven of them transfer electrons between the flavin and the quinone-binding site, and one is on the opposite side of the flavin. Reduction of the iron-sulfur clusters in mitochondrial NADH:ubiquinone oxidoreductase (complex I) by the very low potential reductant EuII-diethylenetriamine-N,N,N',N'',N''-pentaacetate
Fe
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iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit
Fe
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signal shape and g values of cluster N4 [4Fe(G)C], are particularly sensitive to the changes of the environment around N4
Fe2+
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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
Fe2+
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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
Fe2+
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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
Iron
-
contains 4 major iron centers, contains 16-18 gatoms of iron per 650000 Da enzyme
Iron
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enzyme contains Fe-S clusters; the NADH:ubiquinone oxidoreductase complex is composed of three distinct fragments: 1. IP: a water soluble Fe-S-protein that is composed of 5-6 polypeptides and contains four Fe-S clusters, 2. FP: a water-soluble Fe-S-flavoprotein that is composed of three polypeptides and contains FMN and two Fe-S clusters, 3. a water-insoluble fraction containing phospholipids and hydrophobic polypeptides
Iron
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at least 4 different species of low-potential iron-sulfur clusters, characterization of the Fe-S clusters
Iron
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enzyme contains 10.6 atoms of iron and 12.7 atoms of sulfur per dodecamer
Iron
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2 binuclear and 3 tetranuclear EPR detectable iron-sulfur clusters. Cluster N-1a is the most labile component among the five iron sulfur clusters; enzyme contains Fe-S clusters
Iron
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the enzyme contains at least 5 EPR-visible iron-sulfur clusters. The NQO3 subunits contains at least two distinct iron-sulfur clusters: 1 [2Fe-2S] cluster with axial EPR signals and a [4Fe-4S] cluster with rhombic symmetry. The midpoint redox potentials of [2Fe-2S] and [4Fe-4S] clusters at pH 8.6 is -472 mV and -391 mV, respectively
Iron
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enzyme complex contains up to 8 iron-sulfur clusters, 2 * [2Fe-2S] and 6 * [4Fe-4S]
Iron
-
the enzyme contains at most nine putative iron-sulfur cluster binding sites, the NQO2 subunit bears a single [2Fe-2S] cluster, the NQO3 subunit contains multiple iron-sulfur clusters: one [2Fe-2S] cluster, one [4Fe-4S] cluster and possibly another [4Fe-4S] cluster
Iron
-
the CXXCXXXCX27C motif in the NQO3 subunit most likely ligates the [4Fe-4S] cluster
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxy-5-propyloctyl]octahydro-2,2'-bifuran-5-yl]-5-propylnonan-1-ol
-
IC50: 870 nM
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyethyl]octahydro-2,2'-bifuran-5-yl]undecan-1-ol
-
IC50: 280 nM
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyheptyl]octahydro-2,2'-bifuran-5-yl]pentadecan-1-ol
-
IC50: 34 nM
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyheptyl]octahydro-2,2'-bifuran-5-yl]undecan-1-ol
-
IC50: 3.2 nM
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxynonyl]octahydro-2,2'-bifuran-5-yl]tridecan-1-ol
-
IC50: 7.5 nM
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxypropyl]octahydro-2,2'-bifuran-5-yl]undecan-1-ol
-
IC50: 45 nM
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundec-3-yn-1-yl]octahydro-2,2'-bifuran-5-yl]dodec-4-yn-1-ol
-
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(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]dodecan-1-ol
-
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(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]undeca-3,5,7,9-tetrayn-1-ol