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Information on EC 1.6.99.3 - NADH dehydrogenase
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1.6.99.3 NADH dehydrogenaseIUBMB Comments
A flavoprotein containing iron-sulfur centres. After preparations have been subjected to certain treatments, cytochrome c may act as an acceptor. Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. Present in a mitochondrial complex as EC 7.1.1.2, NADH:ubiquinone reductase (H+-translocating).
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Word Map
- 1.6.99.3
- succinate
- microsomal
- mtdnas
- ubiquinone
- trna
- rotenone
- flavoproteins
- flavin
- malate
-
iron-sulfur
-
submitochondrial
- antimycin
- fmn
- ferricyanide
- aniline
- aminopyrine
-
nadh:ubiquinone
-
subcomplexes
- n-demethylase
- leber
-
heteroplasmic
- echinococcus
-
nadh-cytochrome
- granulosus
- semiquinone
-
drug-metabolizing
-
mitochondrial-encoded
-
monophyly
-
phylogeography
-
pleistocene
-
ubiquinol-cytochrome
-
homoplasmic
-
mtdna-encoded
- echinococcosis
-
d-loop
- ethylmorphine
-
succinate-cytochrome
- encephalomyopathy
- leigh
- hydatid
- myxothiazol
- quinol
- hexobarbital
-
pentatricopeptide
-
ethoxycoumarin
-
apocytochrome
-
p-nitroanisole
-
haplogroups
- benzphetamine
-
coiii
The enzyme appears in viruses and cellular organisms
Synonyms
alkyl hydroperoxide reductase, beta-NADH dehydrogenase, cytochrome c reductase, dehydrogenase, reduced nicotinamide adenine dinucleotide, diaphorase, dihydrocodehydrogenase I dehydrogenase, dihydronicotinamide adenine dinucleotide dehydrogenase, diphosphopyridine diaphorase, DPNH dehydrogenase, DPNH diaphorase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkyl hydroperoxide reductase
-
-
-
-
beta-NADH dehydrogenase
-
-
-
-
cytochrome c reductase
-
-
-
-
dehydrogenase, reduced nicotinamide adenine dinucleotide
-
-
-
-
diaphorase
dihydrocodehydrogenase I dehydrogenase
-
-
-
-
dihydronicotinamide adenine dinucleotide dehydrogenase
-
-
-
-
diphosphopyridine diaphorase
-
-
-
-
DPNH dehydrogenase
-
-
-
-
DPNH diaphorase
-
-
-
-
EC 1.6.2.1
-
-
formerly
-
H(2)O(2) forming NADH oxidase
-
-
-
-
NADH dehydrogenase-like complex
NADH diaphorase
-
-
-
-
NADH hydrogenase
-
-
-
-
NADH oxidoreductase
-
-
-
-
NADH-menadione oxidoreductase
-
-
-
-
NADH:oxygen oxidoreductase
-
-
-
-
NDH
NOXase
-
-
-
-
proteins, specific or class, gene MURF3
-
-
-
-
reduced diphosphopyridine nucleotide diaphorase
-
-
-
-
TM0386
type I dehydrogenase
-
-
-
-
diaphorase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADH + H+ + acceptor = NAD+ + reduced acceptor
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
NADH:acceptor oxidoreductase
A flavoprotein containing iron-sulfur centres. After preparations have been subjected to certain treatments, cytochrome c may act as an acceptor. Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. Present in a mitochondrial complex as EC 7.1.1.2, NADH:ubiquinone reductase (H+-translocating).
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CAS REGISTRY NUMBER
COMMENTARY
9079-67-8
-
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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
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
NADH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NAD+ + ?
-
-
-
-
?
NADH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NAD+ + ?
-
-
-
-
?
NADH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NAD+ + ?
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
specific for NADH
-
-
-
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
-
-
-
-
?
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
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NADP+ + ?
-
rate of oxidation is less than 5% of the reaction with NADH
-
-
?
NADPH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NADP+ + ?
-
less than 6% of the activity with NADH
-
-
?
NADPH + 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
NADP+ + ?
-
less than 6% of the activity with NADH
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
activity with NADPH is about 35% of the activity with NADH
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
less active as NADH
-
-
?
additional information
?
-
-
the enzyme also shows NADH oxidase activity
-
-
-
additional information
?
-
-
the enzyme is localized at the main point of electron entry into the respiratory chain. The enzyme catalyzes the transfer of electrons from NADH to the respiratory electron transport components and hence links the major catabolic and energy-producing pathways
-
-
-
additional information
?
-
-
the enzyme transfers electrons from NADH to external oxidants like ferricyanide through pathways which are linked to metabolic processess in the cell
-
-
-
additional information
?
-
-
with anaerobic NO2-, the most downregulated genes are those involved postglycolytically and include many tricarboxylic acid cycle genes and those involved in the electron transport chain, especially those encoding the NADH dehydrogenase I complex, overview
-
-
-
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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
additional information
?
-
-
the enzyme is localized at the main point of electron entry into the respiratory chain. The enzyme catalyzes the transfer of electrons from NADH to the respiratory electron transport components and hence links the major catabolic and energy-producing pathways
-
-
-
additional information
?
-
-
the enzyme transfers electrons from NADH to external oxidants like ferricyanide through pathways which are linked to metabolic processess in the cell
-
-
-
additional information
?
-
-
with anaerobic NO2-, the most downregulated genes are those involved postglycolytically and include many tricarboxylic acid cycle genes and those involved in the electron transport chain, especially those encoding the NADH dehydrogenase I complex, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
natural prosthetic group of the enzyme, apoenzyme catalyzed reaction with ferricyanide, FAD is required for reaction with 2,6-dichlorophenol or with cytochrome c, Km: 0.00056 mM
FAD
1:1 binding stoichiometry with protein and an association constant K of 70000 per mol. The FAD-protein interaction is energetically favorable and the addition of FAD is not necessary to induce the enzyme folded state
NADPH
-
less than 6% of the activity with NADH in reaction with 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ferricyanide
-
competitive substrate inhibition due to its direct binding to the enzyme and forming an inactive binary complex
NAD+
FAD-dependent oxidase activity of NADH dehydrogenase is inhibited by NAD+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
activation of the enzyme in erythrocytes by beta-adrenergic agonists
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
benzyl viologen
-
after induction with 1.5% arabinose in culture medium
0.44
methyl viologen
-
after induction with 1.5% arabinose in culture medium
1.035
NADPH
-
reaction with 3-(4',5'-dimethylthiazol-2-yl)-diphenyltetrazolium bromide
0.06
ferricyanide
-
after induction with 1.5% arabinose in culture medium
0.0692
NADH
-
reaction with 3-(4',5'-dimethylthiazol-2-yl)-diphenyltetrazolium bromide
0.1
NADH
-
electron acceptor benzyl viologen, after induction with 1.5% arabinose in culture medium
0.22
NADH
-
electron acceptor methyl viologen, after induction with 1.5% arabinose in culture medium
0.31
NADH
-
electron acceptor ferricyanide, after induction with 1.5% arabinose in culture medium
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
650
NADH
-
electron acceptor methyl viologen, after induction with 1.5% arabinose in culture medium
725
NADH
-
electron acceptor benzyl viologen, after induction with 1.5% arabinose in culture medium
1170
NADH
-
electron acceptor ferricyanide, after induction with 1.5% arabinose in culture medium
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
-
substrate Clostridium acetobutylicum ferredoxin, after induction with 1.5% arabinose in culture medium
392
-
substrate methyl viologen, after induction with 1.5% arabinose in culture medium
582
-
substrate benzyl viologen, after induction with 1.5% arabinose in culture medium
604
-
substrate ferricyanide, after induction with 1.5% arabinose in culture medium
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8
-
activity with 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
activity with 3-(4',5'-dimethyl-thiazol-2-yl)2,4-diphenyltetrazolium bromide
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes nuoD, nuoG, nuoM encoding components of the NADH dehydrogenase complex
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
digestion of muscle preparation at 37°C with sake-venom phospholipase
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
-
chloroplast and cyanobacterial NDHs have an electron donor-binding subcomplex that is unique to oxygenic photosynthetic organisms, backbone structure of NDH complex common in cyanobacteria and chloroplasts compared to NDH-1 in membranes in heterotrophic bacteria
evolution
-
chloroplast and cyanobacterial NDHs have an electron donor-binding subcomplex that is unique to oxygenic photosynthetic organisms, backbone structure of NDH complex common in cyanobacteria and chloroplasts compared to NDH-1 in membranes in heterotrophic bacteria
evolution
-
chloroplast and cyanobacterial NDHs have an electron donor-binding subcomplex that is unique to oxygenic photosynthetic organisms, backbone structure of NDH complex common in cyanobacteria and chloroplasts compared to NDH-1 in membranes in heterotrophic bacteria
evolution
-
chloroplast and cyanobacterial NDHs have an electron donor-binding subcomplex that is unique to oxygenic photosynthetic organisms, backbone structure of NDH complex common in cyanobacteria and chloroplasts compared to NDH-1 in membranes in heterotrophic bacteria
evolution
-
chloroplast and cyanobacterial NDHs have an electron donor-binding subcomplex that is unique to oxygenic photosynthetic organisms, backbone structure of NDH complex common in cyanobacteria and chloroplasts compared to NDH-1 in membranes in heterotrophic bacteria
physiological function
-
the chloroplast NADH dehydrogenase-like complex shows similarity to complex I in respiratory electron transport, and is involved in electron transport from photoproduced stromal reductants such as NADPH and ferredoxin to the intersystem plastoquinone pool. Chloroplast NDH may also be involved in the electron transport from stromal reductants to oxygen in chlororesipiration. Photosynthetic NDH apparently lacks subunits involved in electron input
physiological function
-
the chloroplast NADH dehydrogenase-like complex shows similarity to complex I in respiratory electron transport, and is involved in electron transport from photoproduced stromal reductants such as NADPH and ferredoxin to the intersystem plastoquinone pool. Chloroplast NDH may also be involved in the electron transport from stromal reductants to oxygen in chlororesipiration. Photosynthetic NDH apparently lacks subunits involved in electron input
physiological function
-
the chloroplast NADH dehydrogenase-like complex shows similarity to complex I in respiratory electron transport, and is involved in electron transport from photoproduced stromal reductants such as NADPH and ferredoxin to the intersystem plastoquinone pool. Chloroplast NDH may also be involved in the electron transport from stromal reductants to oxygen in chlororesipiration. Photosynthetic NDH apparently lacks subunits involved in electron input
physiological function
-
the chloroplast NADH dehydrogenase-like complex shows similarity to complex I in respiratory electron transport, and is involved in electron transport from photoproduced stromal reductants such as NADPH and ferredoxin to the intersystem plastoquinone pool. Chloroplast NDH may also be involved in the electron transport from stromal reductants to oxygen in chlororesipiration. Photosynthetic NDH apparently lacks subunits involved in electron input
physiological function
-
the chloroplast NADH dehydrogenase-like complex shows similarity to complex I in respiratory electron transport, and is involved in electron transport from photoproduced stromal reductants such as NADPH and ferredoxin to the intersystem plastoquinone pool. Chloroplast NDH may also be involved in the electron transport from stromal reductants to oxygen in chlororesipiration. Photosynthetic NDH apparently lacks subunits involved in electron input
additional information
-
backbone structure of NDH complex, overview. Subcomplex structure of flowering plant NDH with specific subunits, four distinct subcomplexes: A, B, membrane-localized and lumen-localized subcomplexes. Dependence of the accumulation of nuclear-encoded NdhM-NdhO on that of NdhH-NdhL, and vice versa
additional information
-
backbone structure of NDH complex, overview. Subcomplex structure of flowering plant NDH with specific subunits, four distinct subcomplexes: A, B, membrane-localized and lumen-localized subcomplexes. Dependence of the accumulation of nuclear-encoded NdhM-NdhO on that of NdhH-NdhL, and vice versa
additional information
-
backbone structure of NDH complex, overview. Subcomplex structure of flowering plant NDH with specific subunits, four distinct subcomplexes: A, B, membrane-localized and lumen-localized subcomplexes. Dependence of the accumulation of nuclear-encoded NdhM-NdhO on that of NdhH-NdhL, and vice versa
additional information
-
backbone structure of NDH complex, overview. Subcomplex structure of flowering plant NDH with specific subunits, four distinct subcomplexes: A, B, membrane-localized and lumen-localized subcomplexes. Dependence of the accumulation of nuclear-encoded NdhM-NdhO on that of NdhH-NdhL, and vice versa
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Yarrowia lipolytica (strain CLIB 122 / E 150)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Yarrowia lipolytica (strain CLIB 122 / E 150)
Yarrowia lipolytica (strain CLIB 122 / E 150)
Yarrowia lipolytica (strain CLIB 122 / E 150)
Yarrowia lipolytica (strain CLIB 122 / E 150)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
additional information
-
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
additional information
-
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
additional information
-
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH. NDH subunits form three types of complexes with different subunit compositions. NDH-1L is required for heterotrophic growth, probably via respiration and CET, while NDH-1M and NDH-1S form the NDH-1MS complex that functions in CO2 concentration
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
0.0004 mg phospholipid per mg of protein, most of which is cardiolipin with traces of phosphatidylethanolamine and phosphatidylglycerol
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G478A
-
no NADH dehydrogenase activity and NADH oxidase activity which appears to result from
K308A
one third of oxidase activity of the wild type NADH dehydrogenase
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, active protein as well as individual subunits are expressed separately
-
expression in Escherichia coli
genes nuoD, nuoG, nuoM encoding components of the NADH dehydrogenase complex, construction of a signature-tagged mutagenesis library of Pseudomonas aeruginosa, genes regulated by NO2-, anaerobically induced, transcriptional profiling, overview
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
6-fold upregulation is induced by a short oxygen exposure
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Adachi, K.; Okuyama, T.
Study on the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. I. Crystallization and properties of the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes
Biochim. Biophys. Acta
268
629-637
1972
Bos taurus
brenda
Kaniuga, Z.
The Transformation of mitochondrial NADH dehydrogenase into NADH:cytochrome c oxidoreductase
Biochim. Biophys. Acta
73
550-564
1963
Sus scrofa
brenda
Wang, C.S.
Human erythrocyte NADH: (acceptor) oxidoreductase. Kinetic properties and competitive substrate inhibition by ferricyanide
Biochim. Biophys. Acta
616
22-29
1980
Homo sapiens
brenda
Kitajima, S.; Yasukochi, Y.; Minakami, S.
Purification and properties of human erythrocyte membrane NADH-cytochrome b5 reductase
Arch. Biochem. Biophys.
210
330-339
1981
Homo sapiens
brenda
Borneleit, P.; Kleber, H.P.
Purification and properties of the membrane-bound NADH dehydrogenase from hydrocarbon-grown acinetobacter calcoaceticus
Biochim. Biophys. Acta
722
94-101
1983
Acinetobacter calcoaceticus
-
brenda
Nisimoto, Y.; Wilson, E.; Heyl, B.L.; Lambeth, J.D.
NADH dehydrogenase from bovine neutrophil membranes. Purification and properties
J. Biol. Chem.
261
285-290
1986
Bos taurus
brenda
Bergsma, J.; van Dongen, M.B.M.; Konings, W.N.
Purification and characterization of NADH dehydrogenase from Bacillus subtilis
Eur. J. Biochem.
128
151-157
1982
Bacillus subtilis, Bacillus subtilis W23
brenda
Ramanarayanan, M.; Rao, N.A.; Vaidyanathan, C.S.
Purification & properties of a soluble reduced nicotinamide adenine dinucleotide (NADH) dehydrogenase from Agrobacterium tumefaciens
Indian J. Biochem. Biophys.
8
214-218
1971
Agrobacterium tumefaciens
brenda
Marques, F.; Bicho, M.P.
Activation of a NADH dehydrogenase in the human erythrocyte by beta-adrenergic agonists: possible involvement of a G protein in enzyme activation
Biol. Signals
6
52-61
1997
Homo sapiens
brenda
Thiagalingam, S.; Yang, T.
Purification and characterization of NADH dehydrogenase from Bacillus megaterium
Can. J. Microbiol.
39
826-833
1993
Bacillus megaterium
-
brenda
Shiraki, M.; Koyama, N.
Involvement of glycine and aspartate residues in the binding capacity of FAD in the NADH dehydrogenase from an alkaliphilic Bacillus
Curr. Microbiol.
46
432-434
2003
Bacillus aciditolerans
brenda
Kitazume, Y.; Mutoh, M.; Shiraki, M.; Koyama, N.
Involvement of Lys-308 in the FAD-dependent oxidase activity of NADH dehydrogenase from an alkaliphilic Bacillus
Res. Microbiol.
157
956-959
2006
Bacillus sp. (in: Bacteria) (P26829), Bacillus sp. (in: Bacteria) YN-1 (P26829)
brenda
Chakraborty, S.; Sakka, M.; Kimura, T.; Sakka, K.
Two proteins with diaphorase activity from Clostridium thermocellum and Moorella thermoacetica
Biosci. Biotechnol. Biochem.
72
877-879
2008
Moorella thermoacetica
brenda
Platt, M.D.; Schurr, M.J.; Sauer, K.; Vazquez, G.; Kukavica-Ibrulj, I.; Potvin, E.; Levesque, R.C.; Fedynak, A.; Brinkman, F.S.; Schurr, J.; Hwang, S.H.; Lau, G.W.; Limbach, P.A.; Rowe, J.J.; Lieberman, M.A.; Barraud, N.; Webb, J.; Kjelleberg, S.; Hunt, D.F.; Hassett, D.J.
Proteomic, microarray, and signature-tagged mutagenesis analyses of anaerobic Pseudomonas aeruginosa at pH 6.5, likely representing chronic, late-stage cystic fibrosis airway conditions
J. Bacteriol.
190
2739-2758
2008
Pseudomonas aeruginosa
brenda
Do, P.M.; Angerhofer, A.; Hrdy, I.; Bardonova, L.; Ingram, L.O.; Shanmugam, K.T.
Engineering Escherichia coli for fermentative dihydrogen production: potential role of NADH-ferredoxin oxidoreductase from the hydrogenosome of anaerobic protozoa
Appl. Biochem. Biotechnol.
153
21-33
2009
Trichomonas vaginalis
brenda
Villegas, J.M.; Torres-Bugeau, C.M.; Chehin, R.; Burgos, M.I.; Fidelio, G.D.; Rintoul, M.R.; Rapisarda, V.A.
Maintenance and thermal stabilization of NADH dehydrogenase-2 conformation upon elimination of its C-terminal region
Biochimie
95
382-387
2013
Arabidopsis thaliana, Marchantia polymorpha, Nicotiana tabacum, Synechocystis sp., Zea mays
brenda
Villegas, J.M.; Valle, L.; Moran Vieyra, F.E.; Rintoul, M.R.; Borsarelli, C.D.; Rapisarda, V.A.
FAD binding properties of a cytosolic version of Escherichia coli NADH dehydrogenase-2
Biochim. Biophys. Acta
1844
576-584
2014
Escherichia coli (P00393)
brenda
Lakhal, R.; Auria, R.; Davidson, S.; Ollivier, B.; Durand, M.; Dolla, A.; Hamdi, M.; Combet-Blanc, Y.
Oxygen uptake rates in the hyperthermophilic anaerobe Thermotoga maritima grown in a bioreactor under controlled oxygen exposure Clues to its defence strategy against oxidative stress
Arch. Microbiol.
193
429-438
2011
Thermotoga maritima (Q9WYL7), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WYL7)
brenda
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