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Information on EC 7.1.1.2 - NADH:ubiquinone reductase (H+-translocating)
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7.1.1.2 NADH:ubiquinone reductase (H+-translocating)IUBMB Comments
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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dinuclear
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luminescence
- 1-methyl-4-phenylpyridinium
-
copperii
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photoluminescence
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high-spin
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
107364096, 13 kDa differentiation-associated protein, AIF-homologous mitochondrion-associated inducer of death, AIFM1, AIFM2, alternative complex I, alternative NADH oxidoreductase, alternative NADH: ubiquinone oxidoreductase, alternative NADH:ubiquinone oxidoreductase, AMAPOR, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
13 kDa differentiation-associated protein
-
-
-
-
alternative NADH:ubiquinone oxidoreductase
artificial mediator accepting pyridine nuclöeotide oxidoreductase
-
-
CDA016
-
-
-
-
Cell adhesion protein SQM1
-
-
-
-
Cell death-regulatory protein GRIM-19
-
-
-
-
CGI-39
-
-
-
-
CI-11KD
-
-
-
-
CI-12KD
-
-
-
-
CI-14.8KD
-
-
-
-
CI-14KD
-
-
-
-
CI-15 kDa
-
-
-
-
CI-16KD
-
-
-
-
CI-17.3KD
-
-
-
-
CI-17.8KD
-
-
-
-
CI-18 kDa
-
-
-
-
CI-18Kd
-
-
-
-
CI-19.3KD
-
-
-
-
CI-19KD
-
-
-
-
CI-20KD
-
-
-
-
CI-21KD
-
-
-
-
CI-22.5Kd
-
-
-
-
CI-23KD
-
-
-
-
CI-27KD
-
-
-
-
CI-28.5KD
-
-
-
-
CI-29.9KD
-
-
-
-
CI-29KD
-
-
-
-
CI-30KD
-
-
-
-
CI-31KD
-
-
-
-
CI-38.5KD
-
-
-
-
CI-39KD
-
-
-
-
CI-40KD
-
-
-
-
CI-42.5KD
-
-
-
-
CI-42KD
-
-
-
-
CI-49KD
-
-
-
-
CI-51KD
-
-
-
-
CI-75KD
-
-
-
-
CI-78KD
-
-
-
-
CI-9.5
-
-
-
-
CI-9KD
-
-
-
-
CI-AGGG
-
-
-
-
CI-AQDQ
-
-
-
-
CI-ASHI
-
-
-
-
CI-B12
-
-
-
-
CI-B14
-
-
-
-
CI-B14.5a
-
-
-
-
CI-B14.5b
-
-
-
-
CI-B15
-
-
-
-
CI-B16.6
-
-
-
-
CI-B17
-
-
-
-
CI-B17.2
-
-
-
-
CI-B18
-
-
-
-
CI-B22
-
-
-
-
CI-B8
-
-
-
-
CI-B9
-
-
-
-
CI-KFYI
-
-
-
-
CI-MLRQ
-
-
-
-
CI-MNLL
-
-
-
-
CI-MWFE
-
-
-
-
CI-PDSW
-
-
-
-
CI-PGIV
-
-
-
-
CI-SGDH
-
-
-
-
CIB17.2
-
-
-
-
coenzyme Q reductase
-
-
-
-
complex 1
complex I
complex I (electron transport chain)
-
-
-
-
complex I (mitochondrial electron transport)
-
-
-
-
complex I (NADH:Q1 oxidoreductase)
-
-
-
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complex I dehydrogenase
-
-
-
-
Complex I-11KD
-
-
-
-
Complex I-12KD
-
-
-
-
Complex I-14.8KD
-
-
-
-
Complex I-14KD
-
-
-
-
Complex I-15 kDa
-
-
-
-
Complex I-16KD
-
-
-
-
Complex I-17.3KD
-
-
-
-
Complex I-17.8KD
-
-
-
-
Complex I-18 kDa
-
-
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-
Complex I-18Kd
-
-
-
-
Complex I-19.3KD
-
-
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-
Complex I-19KD
-
-
-
-
Complex I-20KD
-
-
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-
Complex I-21KD
-
-
-
-
Complex I-22.5Kd
-
-
-
-
Complex I-23KD
-
-
-
-
Complex I-27KD
-
-
-
-
Complex I-28.5KD
-
-
-
-
Complex I-29.9KD
-
-
-
-
Complex I-29KD
-
-
-
-
Complex I-30KD
-
-
-
-
Complex I-38.5KD
-
-
-
-
Complex I-39KD
-
-
-
-
Complex I-40KD
-
-
-
-
Complex I-42.5KD
-
-
-
-
Complex I-42KD
-
-
-
-
Complex I-49KD
-
-
-
-
Complex I-51KD
-
-
-
-
Complex I-75KD
-
-
-
-
Complex I-78KD
-
-
-
-
Complex I-9.5KD
-
-
-
-
Complex I-9KD
-
-
-
-
Complex I-AGGG
-
-
-
-
Complex I-AQDQ
-
-
-
-
Complex I-ASHI
-
-
-
-
Complex I-B12
-
-
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Complex I-B14
-
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Complex I-B14.5a
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-
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-
Complex I-B14.5b
-
-
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Complex I-B15
-
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-
-
Complex I-B16.6
-
-
-
-
Complex I-B17
-
-
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Complex I-B17.2
-
-
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Complex I-B18
-
-
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Complex I-B22
-
-
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Complex I-B8
-
-
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Complex I-B9
-
-
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Complex I-KFYI
-
-
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Complex I-MLRQ
-
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Complex I-MNLL
-
-
-
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Complex I-MWFE
-
-
-
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Complex I-PDSW
-
-
-
-
Complex I-PGIV
-
-
-
-
Complex I-SGDH
-
-
-
-
dihydronicotinamide adenine dinucleotide-coenzyme Q reductase
-
-
-
-
DPNH-coenzyme Q reductase
-
-
-
-
DPNH-ubiquinone reductase
-
-
-
-
electron transfer complex I
-
-
-
-
Gene associated with retinoic-interferon-induced mortality 19 protein
-
-
-
-
GGHPW
-
-
-
-
GRIM-19
-
-
-
-
Hypothetical protein Walter
-
-
-
-
Internal NADH dehydrogenase
mitochondrial complex I
mitochondrial electron transport complex 1
-
-
-
-
mitochondrial electron transport complex I
-
-
-
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mitochondrial NADH:ubiquinone oxidoreductase
Nad1
NADH coenzyme Q1 reductase
-
-
-
-
NADH dehydrogenase
NADH-coenzyme Q oxidoreductase
-
-
-
-
NADH-coenzyme Q reductase
-
-
-
-
NADH-CoQ oxidoreductase
NADH-CoQ reductase
-
-
-
-
NADH-ferricyanide reductase
-
-
-
-
NADH-Q6 oxidoreductase
-
-
-
-
NADH-quinone oxidoreductase
NADH-quinone reductase
NADH-ubiquinone oxidoreductase
NADH-ubiquinone reductase
NADH-ubiquinone-1 reductase
-
-
-
-
NADH:HAR reductase
NADH:Q oxidoreductase
NADH:ubiquinone oxidoreductase
NADH:ubiquinone oxidoreductase complex
-
-
-
-
ND1
NDH
NDH-1
NDH-2
NDH-2A
NDH2
Ndi1p
NrcN
PAI
Protein P1
-
-
-
-
proton-pumping NADH-ubiquinone oxidoreductase
proton-pumping NADH:ubiquinone oxidoreductase
RCC-I
reduced nicotinamide adenine dinucleotide-coenzyme Q reductase
-
-
-
-
reductase, ubiquinone
-
-
-
-
respiratory chain complex I
respiratory complex I
TT_C1484
type I dehydrogenase
-
-
-
-
type I NADH dehydrogenase
type II NADH dehydrogenase
ubiquinone reductase
-
-
-
-
Ubiquinone-binding protein
-
-
-
-
complex I
-
-
complex I
-
-
complex I
-
-
complex I
-
-
Internal NADH dehydrogenase
-
-
-
-
NADH-CoQ oxidoreductase
-
-
-
-
NADH-quinone reductase
-
-
-
-
NADH-ubiquinone oxidoreductase
-
-
-
-
NADH-ubiquinone oxidoreductase
-
-
NADH-ubiquinone reductase
-
-
-
-
NADH:Q oxidoreductase
-
-
-
-
NADH:ubiquinone oxidoreductase
-
-
NADH:ubiquinone oxidoreductase
-
-
NADH:ubiquinone oxidoreductase
-
-
NDH-1
-
the NuoG subunit of the type I NADH dehydrogenase
-
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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
-
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
-
NADH + ubiquinone + 6 H+[side 1] = NAD+ + ubiquinol + 7 H+[side 2]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
redox reaction
-
-
-
-
redox reaction
-
no indication for primary or secondary Na+ translocation
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
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
aerobic respiration (NDH-1 to cytochrome c oxidase via plastocyanin), aerobic respiration I (cytochrome c), aerobic respiration III (alternative oxidase pathway), Fe(II) oxidation, NAD(P)/NADPH interconversion, NADH to cytochrome bd oxidase electron transfer I, NADH to cytochrome bo oxidase electron transfer I
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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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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
-
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-NADH + ubiquinone + H+[side 1]
deamino-NAD+ + ubiquinol + H+[side 2]
-
-
-
-
?
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+ + 2,3-dimethoxy-5-methyl-6-[(6-methylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]benzene-1,4-diol
-
-
-
-
?
NADH + 2,3-dimethoxy-5-methyl-6-[(6-phenylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]benzo-1,4-quinone
NAD+ + 2,3-dimethoxy-5-methyl-6-[(6-phenylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]benzene-1,4-diol
-
-
-
-
?
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+ + 2-[(2,6-dimethylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzene-1,4-diol
-
-
-
-
?
NADH + 2-[(2-chloro-6-methylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
NAD+ + 2-[(2-chloro-6-methylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzene-1,4-diol
-
-
-
-
?
NADH + 2-[(2-chloro-6-phenylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
NAD+ + 2-[(2-chloro-6-phenylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzene-1,4-diol
-
-
-
-
?
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+ + 2-[(6-chloro-2,3-dihydroimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzene-1,4-diol
-
-
-
-
?
NADH + 2-[(6-chloro-2-methylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
NAD+ + 2-[(6-chloro-2-methylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzene-1,4-diol
-
-
-
-
?
NADH + 2-[(6-chloroimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
NAD+ + 2-[(6-chloroimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzene-1,4-diol
-
-
-
-
?
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+
-
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+ + 2-methylnaphthalene-1,4-diol
-
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
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
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
?
-
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 + 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
-
-
?
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 SUBSTRATE
NATURAL 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
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
?
-
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
Ubiquinone-10
-
the enzyme contains 4.2-4.5 mol of ubiquinone-10 per 650000 Da enzyme
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
FAD content of homologously produced NrcN is 1 mol of FAD/mol protein. FAD is not covalently bound
FAD
UV-Vis spectrum shows a shoulder at 465 nm. FAD is not covalently bound
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
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
NADH
-
-
NADH
-
-
392678, 392681, 392682, 392692, 392718, 392831, 659206, 659331, 671940, 672008, 672041, 672043, 672349, 673614, 673620, 673940, 674624, 675494, 696380, 724310, 725142, 725517
NADH
-
-
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, 711290, 714281, 714993, 724564, 725002, 725003, 725491
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
-
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
-
the adenosine moiety is crucial for binding, while the nicotinamide is detrimental to binding
NADH
-
the NADH binding site is located in the matrix of mitochondria and their inner membrane is impermeable for NADH
NADPH
-
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
-
the enzyme contains only substoichiometric amounts of ubiquinone-9, 0.2-0.4 mol/mol
-
additional information
-
[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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe-S
Fe2+
Iron
Mg2+
[4Fe-4S] center
additional information
-
no FeS clusters are present in the protein
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
-
iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit
Fe
-
signal shape and g values of cluster N4 [4Fe(G)C], are particularly sensitive to the changes of the environment around N4
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
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
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
Iron
-
contains 4 major iron centers, contains 16-18 gatoms of iron per 650000 Da enzyme
Iron
-
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
-
at least 4 different species of low-potential iron-sulfur clusters, characterization of the Fe-S clusters
Iron
-
enzyme contains 10.6 atoms of iron and 12.7 atoms of sulfur per dodecamer
Iron
-
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
-
enzyme complex contains up to 8 iron-sulfur clusters, 2 * [2Fe-2S] and 6 * [4Fe-4S]
Iron
-
2 binuclear and 3 tetranuclear EPR detectable iron-sulfur clusters. Cluster N-1a is the most labile component among the five iron sulfur clusters
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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INHIBITOR
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
-
-
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]dodecan-1-ol
-
-
(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
-
IC50: 0.000172 mM
(1R)-1-[(2R,2'R,5R,5'R)-5'-[(1R)-5-ethyl-1-hydroxyoctyl]octahydro-2,2'-bifuran-5-yl]undecan-1-ol
-
IC50: 27 nM
(1R)-5-ethyl-1-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxy-5-propyloctyl]octahydro-2,2'-bifuran-5-yl]octan-1-ol
-
IC50: 1500 nM
(1R,1'R)-1,1'-((2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diyl)-bis-(6-(4-n-butylphenoxy)hex-3-yn-1-ol)
-
-
(1R,1'R)-1,1'-((2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diyl)-bis-(6-(4-n-butylphenoxy)hexan-1-ol)
-
-
(1R,1'R)-1,1'-(2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diylbis(5-[4-[(E)-(4-butylphenyl)diazenyl]phenoxy]pentan-1-ol)
-
48 nM, 70% inhibition
(1R,1'R)-1,1'-(2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diylbis(5-[4-[(Z)-(4-butylphenyl)diazenyl]phenoxy]pentan-1-ol)
-
48 nM, 70% inhibition
(1R,1'R)-1,1'-(2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diylbis[6-(2-butylphenoxy)hexan-1-ol]
-
IC50: 1000 nM
(1R,1'R)-1,1'-(2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diylbis[6-(4-butylphenoxy)hexan-1-ol]
-
IC50: 0.83 nM
(1R,1'R)-1,1'-(2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diyldihexan-1-ol
-
IC50: 4500 nM
(1R,1'R)-1,1'-(2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diyldioctan-1-ol
-
IC50: 45 nM
(5S)-3-[(10R)-10-hydroxy-10-[(2R,2'R,5R,5'R)-5'-[(1R)-1 hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]decyl]-5-methylfuran-2(5H)-one
-
IC50: 0.0000012 mM
(5S)-3-[(13R)-13-hydroxy-13-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]tridec-8-yn-1-yl]-5-methylfuran-2(5H)-one
-
IC50: 0.00000083 mM
(5S)-3-[(13R)-13-hydroxy-13-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]trideca-4,6,8,10-tetrayn-1-yl]-5-methylfuran-2(5H)-one
-
IC50: 0.0000017 mM
(5S)-3-[(13R)-13-hydroxy-13-[(2R,2'R,5R,5'R)-5'-[(1S)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]tridec-10-yn-1-yl]-5-methylfuran-2(5H)-one
-
IC50: 0.000001 mM
(5S)-3-[(13R)-13-hydroxy-13-[(2R,2'R,5R,5'R)-5'-[(1S)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]tridec-4-yn-1-yl]-5-methylfuran-2(5H)-one
-
IC50: 0.00000085 mM
(5S)-3-[(13R)-13-hydroxy-13-[(2R,5R)-5-[(1S)-1-hydroxytridecyl]tetrahydrofuran-2-yl]trideca-4,6,8,10-tetrayn-1-yl]-5-methylfuran-2(5H)-one
-
IC50: 0.00028 mM
(5S)-3-[(13R)-13-hydroxy-13-[(2R,5R)-5-[(1S)-1-hydroxytridecyl]tetrahydrofuran-2-yl]tridecyl]-5-methylfuran-2(5H)-one
-
IC50: 0.0000023 mM
(5S)-3-[(13S)-13-hydroxy-13-[(2R,5R)-5-[(1S)-1-hydroxytriecyl]tetrahydrofuran-2-yl]tridecyl]-5-methylfuran-2(5H)-one
-
IC50: 0.0000051 mM
(5S)-3-[(16R)-16-hydroxy-16-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]hexadecyl]-5-methylfuran-2(5H)-one
-
IC50: 0.000013 mM
(5S)-3-[(19R)-19-hydroxy-19-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]nonadecyl]-5-methylfuran-2(5H)-one
-
IC50: 0.000271 mM
(5S)-3-[(2E,13R)-13-hydroxy-13-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]tridec-2-en-4-yn-1-yl]-5-methylfuran-2(5H)-one
-
IC50: 0.0000011 mM
(5S)-3-[(5R)-5-hydroxy-5-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]pentyl]-5-methylfuran-2(5H)-one
-
IC50: 0.000014 mM
(5S)-3-[(7E,13S)-13-hydroxy-13-[(2R,5R)-5-[(1S)-1-hydroxytridecyl]tetrahydrofuran-2-yl]tridec-7-en-9-yn-1-yl]-5-methylfuran-2(5H)-one
-
IC50: 0.0000052 mM
(5S)-3-[(8E,13R)-13-hydroxy-13-[(2R,2'R,5R,5'R)-5'-[(1S)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]tridec-8-en-10-yn-1-yl]-5-methylfuran-2(5H)-one
-
IC50: 0.00000092 mM
(5S)-3-[(8R)-8-hydroxy-8-[(2R,2'R,5R,5'R)-5'-[(1R)-1-hydroxyundecyl]octahydro-2,2'-bifuran-5-yl]octyl]-5-methylfuran-2(5H)-one
-
IC50: 0.0000016 mM
(5S)-3-[4-[(E)-(4-[[(4R)-4-hydroxy-4-[(2R,5R)-5-[(1R)-1-hydroxytridecyl]tetrahydrofuran-2-yl]butyl]oxy]phenyl)diazenyl]benzyl]-5-methylfuran-2(5H)-one
-
-
(5S)-3-[4-[(E)-(4-[[(7R)-7-hydroxy-7-[(2R,5R)-5-[(1R)-1-hydroxytridecyl]tetrahydrofuran-2-yl]heptyl]oxy]phenyl)diazenyl]benzyl]-5-methylfuran-2(5H)-one
-
-
(5S)-3-[4-[(Z)-(4-[[(4R)-4-hydroxy-4-[(2R,5R)-5-[(1R)-1-hydroxytridecyl]tetrahydrofuran-2-yl]butyl]oxy]phenyl)diazenyl]benzyl]-5-methylfuran-2(5H)-one
-
-
(5S)-3-[4-[(Z)-(4-[[(7R)-7-hydroxy-7-[(2R,5R)-5-[(1R)-1-hydroxytridecyl]tetrahydrofuran-2-yl]heptyl]oxy]phenyl)diazenyl]benzyl]-5-methylfuran-2(5H)-one
-
-
1-methyl-4-phenylpyridinium
-
complex I inhibitor, which has no effect on mediobasal hypothalamic tuberoinfundibular dopamine neurons, but significantly increases the percentage of apoptag immunoreactive neurons in midbrain primary nigrostriatal dopamine and mesolimbic dopamine cultures
1-methyl-4-phenylpyridinium ion
-
inhibition of mitochondrial complex I. Neuroprotective effects of caffeine in the MPP+ model of apoptosis are mediated through activation of the ataxia telangiectasia mutated enzyme/p53 pathway. Caffeine decreases the expression of cyclin D and the transcription factor E2F-1, a regulator of apoptosis in neurons. Caffeine-mediated neuroprotection is not mediated through blockade of adenosine receptors because DPCPX and CGS-15943, two antagonists of these receptors, fail to attenuate apoptosis produced by 1-methyl-4-phenylpyridinium ion treatment
2',3'-dideoxycytidine
-
0.001 mM prevents the phosphorylation of the NDUFB11 subunit of complex I
2,3-dimethoxy-5-methyl-6-[(6-methylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]benzo-1,4-quinone
-
0.00028 mM, NADH-coenzyme Q1 activity
2-n-decyl-quinazolin-4-yl-amine
transport is completely sensitive to 2-n-decyl-quinazolin-4-yl-amine
2-[(2,6-dimethylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
-
0.00077 mM, NADH-coenzyme Q1 activity
2-[(6-chloro-2,3-dihydroimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
-
0.00065 mM, NADH-coenzyme Q1 activity
2-[(6-chloro-2-methylimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
-
0.00025 mM, NADH-coenzyme Q1 activity
2-[(6-chloroimidazo[2,1-b][1,3]thiazol-5-yl)methyl]-5,6-dimethoxy-3-methylbenzo-1,4-quinone
-
0.00096 mM, NADH-coenzyme Q1 activity
2-[4-(4-fluorobutyl)benzylsulfanyl]-3-methylchromen-4-one
-
most potent inhibitor. 30 min after high uptake of the radiotracer from the blood pool into the myocardium, kidney, and liver. After 2 h about 66% of the activity in the myocardium at 30 min has been retained, whereas ca. 70% has been cleared from the liver and kidney
3'-azido-3'-deoxythymidine
-
0.01 and 0.05 mM prevent the phosphorylation of the NDUFB11 subunit of complex I. This is associated with a decrease in complex I activity
3'-azido-3'-deoxythymidine monophosphate
-
0.15 mM prevents the phosphorylation of the NDUFB11 subunit of complex I. This is associated with a decrease in complex I activity
5-(N-ethyl-N-isopropyl)-amiloride
-
0.015 mM, up to 40% decrease in the proton pumping activity of the wild-type and subunit NuoL mutants D303A, D400A, D400E, no significant change in mutant D178N
5-fluoro-3-methyl-2-(4-(4-(trifluoromethoxy)benzyl)-phenyl)quinolin-4(1H)-one
inhibitor exhibits potency against both drug-resistant strains in vitro and parasite-infected mice in vivo via a potential allosteric mechanism. Inhibitor can be used in combination with dihydroartemisinin synergistically
5BM-GX
-
inhibits transhydrogenation reaction with NADH and 3'-acetyl pyridine adenine dinucleotide
AMP
-
dead-end inhibitor, linear competitive inhibitor of NADH, linear uncompetitive inhibitor of oxidized 2,6-dichlorophenol indophenol
AMS-GX
-
inhibits transhydrogenation reaction with NADH and 3'-acetyl pyridine adenine dinucleotide
atovaquone
-
20 nM, complete inhibition of partially purified enzyme. Inhibition of complex I represents a likely mechanism of the known antileishmanial activity of the drug
benzo (1,2,3) thiadiazole-7-carbothioic acid S-methyl ester
-
0.075 mM, strong inhibition
bis-tetrahydrofuran acetogenin
-
the additional methylenes enhance the hydrophobicity of the spacer region, which may be thermodynamically advantageous for bringing the polar gamma-lactone ring into the membrane-embedded segment of complex I
-
carvedilol
-
decreases mitochondrial complex I activity, which is associated with an increase in mitochondrial H2O2 production, total glutathione and protein thiols content
diphenyl iodonium
-
maximal inhibition after preincubation with NADH, more complete inhibition with the more hydrophobic electron acceptors such as ubiquinone-1 or ubiquinone-2 as electron acceptor compared to the more hydrophilic ones, such as ubiquinone-0 or dichloroindophenol
diphenyleneiodonium
-
strongly inhibits superoxide production by complex I driven by reverse electron transport from succinate. Inhibition of superoxide production is not dependent on changes in the pH gradient. The inhibitor does not react with the flavin of complex I
DL-homocysteic acid
-
marked (ca. 64%) decrease of respiratory chain complex I activity in the cerebral cortex of immature rats following seizures induced by bilateral intracerebroventricular infusion of DL-homocysteic acid (600 nanomol/side). Decrease is already evident during the acute phase of seizures (60-90 min after infusion) and persists for at least 20 h after the seizures. Inhibition is selective for complex I since activities of complex II and IV and citrate synthase remain unaffected. Inhibition of complex I activity is not associated with changes in complex I content. Enhanced production of reactive oxygen species by inhibited complex I in mitochondria from DL-homocysteic acid-treated animals. Competitive NMDA receptor antagonist AP7, a selective and potent group II mGluR agonist (2R,4R)-APDC and a highly selective group III mGluR, subtype 8, agonist (S)-3,4-DCPG, significantly reduce the extent of complex I inhibition. The superoxide dismutase mimetic Tempol and a selective peroxynitrite scavenger and decomposition catalyst FeTPPS provide a significant attenuation of complex I inhibition associated with DL-homocysteic acid-induced seizures
flutamide
-
inhibits complex I of the electron transport chain to a greater extent than a nitro to cyano analogue of flutamide. As compared to the nitro to cyano analogue of flutamide, the nitroaromatic group of flutamide enhances cytotoxicity to hepatocytes, likely through mechanisms involving mitochondrial dysfunction and ATP depletion that include complex I inhibition
Mersalyl
-
0.3 mM, 77% inhibition of NADH-ubiquinone-1 reductase activity, 96% inhibition of NADH-potassium ferricyanide reductase activity
Mg2+
-
inhibition of the enzyme in its inactive form, in its active form the enzyme complex is not sensitive
NEM
-
inhibition of the enzyme in its inactive form, in its active form the enzyme complex is not sensitive
oxygen
-
O2 induces self-inactivation of the enzyme via the formation of protein radicals
Rhein
-
i.e. 4,5-dioxy-anthraquinone-z-carbonic acid, competes for a NADH-binding site
YLVCGERGFFYTPKA
-
hypoxia causes prolonged inhibition of maximal complex I activity and ultrastructural phenotypes associated with swelling, namely, fading of cristae, intracristal dilations and membrane disruption. Administration of the selective neuronal nitric oxide synthase inhibitor 7-nitroindazole 20 min before hypoxia prevents complex I inhibition in a dose-dependent manner and most ultrastructural damage
(1R,1'R)-1,1'-(2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diyldiundecan-1-ol
-
IC50: 0.0000016 mM
(1R,1'R)-1,1'-(2R,2'R,5R,5'R)-octahydro-2,2'-bifuran-5,5'-diyldiundecan-1-ol
-
IC50: 1.6 nM
2-decyl-4-quinazolinyl amine
-
the compound is both a complex I inhibitor and an uncoupler
5-(N-ethyl-N-isopropyl)amiloride
inhibits of complex I and increases the membrane conductivity
6-azido-4-(4-iodophenethylamino)quinazoline
the compound specifically binds to the 49000 Da and ND1 subunits with a frequency of about 4:1
6-azido-4-(4-iodophenethylamino)quinazoline
-
the compound specifically binds to the 49000 Da and ND1 subunits with a frequency of about 4:1
ADP-ribose
-
ADP-ribose acts as mixed-type inhibitors for NADH, ferricyanide and 5,8-dioxy-1,4-naphthoquinone
Ca2+
-
inhibits complex I activity in a concentration-dependent manner. Ca2+ acts specifically on complex I. Complex I inactivation by Ca2+ results in reduction of NADH-supported electron transport activity and suppression of the rate of O2- production
capsaicin
-
no inhibition of enzymes where the energy couling site is absent
capsaicin
-
and synthetic capsaicin analogue. Several synthetic capsaicins discriminate between NDH-1 and NDH-2 much better than natural capsaicin
capsaicin
-
and synthetic capsaicin analogue. Several synthetic capsaicins discriminate between NDH-1 and NDH-2 much better than natural capsaicin
capsaicin
-
no inhibition of enzymes where the energy couling site is absent
capsaicin
-
and synthetic capsaicin analogue. Several synthetic capsaicins discriminate between NDH-1 and NDH-2 much better than natural capsaicin