1.6.5.9: NADH:quinone reductase (non-electrogenic)
This is an abbreviated version!
For detailed information about NADH:quinone reductase (non-electrogenic), go to the full flat file.
Word Map on EC 1.6.5.9
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1.6.5.9
-
ndh-2
-
hydrogenases
-
proton-translocating
-
ubiquinone-1
-
hqno
-
2-heptyl-4-hydroxyquinoline-n-oxide
-
single-subunit
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deamino-nadh
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na+-translocating
-
rotenone-sensitive
- 1.6.5.9
- ndh-2
- hydrogenases
-
proton-translocating
- ubiquinone-1
- hqno
- 2-heptyl-4-hydroxyquinoline-n-oxide
-
single-subunit
- deamino-nadh
-
na+-translocating
-
rotenone-sensitive
Reaction
Synonyms
alternative external NADH dehydrogenase, alternative NADH dehydrogenase, alternative NADH-quinone oxidoreductase, alternative NADH:quinone reductase, alternative NADH:ubiquinone oxidoreductase, alternative rotenone-insensitive NADH:Q oxidoreductase, CathTA2_0279, Cgl1465, EC 1.6.5.11, EC 1.6.99.5, external alternative NADH dehydrogenase, external alternative NADH: ubiquinone oxidoreductase, external NADH:ubiquinone oxidoreductase, external rotenone-insensitive NADH dehydrogenase, internal alternative NADH dehydrogenase, internal alternative NADH: ubiquinone oxidoreductase, internal alternative NADH:ubiquinone oxidoreductase, Internal NADH dehydrogenase, internal rotenone-insensitive NADH dehydrogenase, NADH dehydrogenase, NADH dehydrogenase-2, NADH-ubiquinone oxidoreductase, NADH: ubiquinone oxidoreductase, NADH: ubiquinone-2 oxidoreductase, NADH:Q6 oxidoreductase, NADH:ubiquinone reductase (non-electrogenic), NADHQ2, NDA, NDB, NdeA, NdeA-B, NDH, NDH-2, NDH-II, NDH2, NDH2e, NDH2i, Ndi1, NdiA, NDX, non-proton pumping type II NADH dehydrogenase, non-proton-pumping NADH dehydrogenase, rotenone-insensitive NADH dehydrogenase, rotenone-insensitive NADH-ubiquinone oxidoreductase
ECTree
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Reference on EC 1.6.5.9 - NADH:quinone reductase (non-electrogenic)
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
De Vries, S.; Grivell, L.A.
Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae
Eur. J. Biochem.
176
377-384
1988
Saccharomyces cerevisiae
Velazquez, I.; Pardo, J.P.
Kinetic characterization of the rotenone-insensitive internal NADH:ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae
Arch. Biochem. Biophys.
389
7-14
2001
Saccharomyces cerevisiae
Garofano, A.; Eschemann, A.; Brandt, U.; Kerscher, S.
Substrate-inducible versions of internal alternative NADH: ubiquinone oxidoreductase from Yarrowia lipolytica
Yeast
23
1129-1136
2006
Yarrowia lipolytica
Murai, M.; Yamashita, T.; Senoh, M.; Mashimo, Y.; Kataoka, M.; Kosaka, H.; Matsuno-Yagi, A.; Yagi, T.; Miyoshi, H.
Characterization of the ubiquinone binding site in the alternative NADH-quinone oxidoreductase of Saccharomyces cerevisiae by photoaffinity labeling
Biochemistry
49
2973-2980
2010
Saccharomyces cerevisiae (P32340), Saccharomyces cerevisiae
Kerscher, S.
Diversity and origin of alternative NADH:ubiquinone oxidoreductases
Biochim. Biophys. Acta
1459
274-283
2000
Saccharomyces pastorianus
Guerrero-Castillo, S.; Vazquez-Acevedo, M.; Gonzalez-Halphen, D.; Uribe-Carvajal, S.
In Yarrowia lipolytica mitochondria, the alternative NADH dehydrogenase interacts specifically with the cytochrome complexes of the classic respiratory pathway
Biochim. Biophys. Acta
1787
75-85
2009
Yarrowia lipolytica (F2Z699), Yarrowia lipolytica
Cook, N.; Cammack, R.
Purification and characterization of the rotenone-insensitive NADH dehydrogenase of mitochondria from Arum maculatum
Eur. J. Biochem.
141
573-577
1984
Arum maculatum
Mogi, T.; Matsushita, K.; Murase, Y.; Kawahara, K.; Miyoshi, H.; Ui, H.; Shiomi, K.; Omura, S.; Kita, K.
Identification of new inhibitors for alternative NADH dehydrogenase (NDH-II): Research Letter
FEMS Microbiol. Lett.
291
157-161
2009
Gluconobacter oxydans, Gluconobacter oxydans NBRC3172
Kerscher, S.; Okun, J.; Brandt, U.
A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica
J. Cell Sci.
112
2347-2354
1999
Yarrowia lipolytica, Yarrowia lipolytica E 150
Kerscher, S.; Eschemann, A.; Okun, P.; Brandt, U.
External alternative NADH: ubiquinone oxidoreductase redirected to the internal face of the mitochondrial inner membrane rescues complex I deficiency in Yarrowia lipolytica
J. Cell Sci.
114
3915-3921
2001
Yarrowia lipolytica
Rasmusson, A.; Svensson, A.; Knoop, V.; Grohmann, L.; Brennicke, A.
Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes: Two enzymes are present in potato mitochondria
Plant J.
20
79-87
1999
Solanum tuberosum, Solanum tuberosum cultivar Desiree
Bahadorani, S.; Cho, J.; Lo, T.; Contreras, H.; Lawal, H.O.; Krantz, D.E.; Bradley, T.J.; Walker, D.W.
Neuronal expression of a single-subunit yeast NADH-ubiquinone oxidoreductase (Ndi1) extends Drosophila lifespan
Aging Cell
9
191-202
2010
Saccharomyces cerevisiae
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
Escherichia coli
Dinamarco, T.; Figueiredo Pimentel, B.; Savoldi, M.; Malavazi, I.; Soriani, F.; Uyemura, S.; Ludovico, P.; Goldman, M.; Goldman, G.
The roles played by Aspergillus nidulans apoptosis-inducing factor (AIF)-like mitochondrial oxidoreductase (AifA) and NADH-ubiquinone oxidoreductases (NdeA-B and NdiA) in farnesol resistance
Fungal Genet. Biol.
47
1055-1069
2010
Aspergillus nidulans
Verner, Z.; Skodova, I.; Polakova, S.; Durisova-Benkovicova, V.; Horvath, A.; Lukes, J.
Alternative NADH dehydrogenase (NDH2): intermembrane-space-facing counterpart of mitochondrial complex I in the procyclic Trypanosoma brucei
Parasitology
140
328-337
2013
Trypanosoma brucei, Trypanosoma brucei 29-13
Iwata, M.; Lee, Y.; Yamashita, T.; Yagi, T.; Iwata, S.; Cameron, A.D.; Maher, M.J.
The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates
Proc. Natl. Acad. Sci. USA
109
15247-15252
2012
Saccharomyces cerevisiae
Dunn, E.A.; Cook, G.M.; Heikal, A.
Annotated compound data for modulators of detergent-solubilised or lipid-reconstituted respiratory type II NADH dehydrogenase activity obtained by compound library screening
Data Brief
6
275-278
2016
Caldalkalibacillus thermarum (F5L3B8), Caldalkalibacillus thermarum TA2.A1 (F5L3B8)
Heikal, A.; Nakatani, Y.; Dunn, E.; Weimar, M.R.; Day, C.L.; Baker, E.N.; Lott, J.S.; Sazanov, L.A.; Cook, G.M.
Structure of the bacterial type II NADH dehydrogenase a monotopic membrane protein with an essential role in energy generation
Mol. Microbiol.
91
950-964
2014
Caldalkalibacillus thermarum (F5L3B8), Caldalkalibacillus thermarum, Caldalkalibacillus thermarum TA2.A1 (F5L3B8)
Matus-Ortega, M.G.; Cardenas-Monroy, C.A.; Flores-Herrera, O.; Mendoza-Hernandez, G.; Miranda, M.; Gonzalez-Pedrajo, B.; Vazquez-Meza, H.; Pardo, J.P.
New complexes containing the internal alternative NADH dehydrogenase (Ndi1) in mitochondria of Saccharomyces cerevisiae
Yeast
32
629-641
2015
Saccharomyces cerevisiae (P32340), Saccharomyces cerevisiae
Maeda, T.; Koch-Koerfges, A.; Bott, M.
Relevance of NADH dehydrogenase and alternative two-enzyme systems for growth of Corynebacterium glutamicum with glucose, lactate, and acetate
Front. Bioeng. Biotechnol.
8
621213
2020
Corynebacterium glutamicum (Q79VG1), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q79VG1)
Gospodaryov, D.V.; Strilbytska, O.M.; Semaniuk, U.V.; Perkhulyn, N.V.; Rovenko, B.M.; Yurkevych, I.S.; Barata, A.G.; Dick, T.P.; Lushchak, O.V.; Jacobs, H.T.
Alternative NADH dehydrogenase extends lifespan and increases resistance to xenobiotics in Drosophila
Biogerontology
21
155-171
2020
Ciona intestinalis
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