BRENDA - Enzyme Database show
show all sequences of 1.6.99.3

Maintenance and thermal stabilization of NADH dehydrogenase-2 conformation upon elimination of its C-terminal region

Villegas, J.M.; Torres-Bugeau, C.M.; Chehin, R.; Burgos, M.I.; Fidelio, G.D.; Rintoul, M.R.; Rapisarda, V.A.; Biochimie 95, 382-387 (2013)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
-
Arabidopsis thaliana
9507
-
chloroplast
-
Marchantia polymorpha
9507
-
chloroplast
-
Nicotiana tabacum
9507
-
chloroplast
-
Zea mays
9507
-
thylakoid membrane
-
Arabidopsis thaliana
42651
-
thylakoid membrane
-
Marchantia polymorpha
42651
-
thylakoid membrane
-
Nicotiana tabacum
42651
-
thylakoid membrane
-
Zea mays
42651
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
-
-
-
Marchantia polymorpha
-
-
-
Nicotiana tabacum
-
-
-
Synechocystis sp.
-
-
-
Zea mays
-
-
-
Subunits
Subunits
Commentary
Organism
More
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
Arabidopsis thaliana
More
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
Marchantia polymorpha
More
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
Nicotiana tabacum
More
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
Synechocystis sp.
More
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
Zea mays
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Arabidopsis thaliana
NADH
-
Marchantia polymorpha
NADH
-
Nicotiana tabacum
NADH
-
Synechocystis sp.
NADH
-
Zea mays
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Arabidopsis thaliana
NADH
-
Marchantia polymorpha
NADH
-
Nicotiana tabacum
NADH
-
Synechocystis sp.
NADH
-
Zea mays
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
-
Arabidopsis thaliana
9507
-
chloroplast
-
Marchantia polymorpha
9507
-
chloroplast
-
Nicotiana tabacum
9507
-
chloroplast
-
Zea mays
9507
-
thylakoid membrane
-
Arabidopsis thaliana
42651
-
thylakoid membrane
-
Marchantia polymorpha
42651
-
thylakoid membrane
-
Nicotiana tabacum
42651
-
thylakoid membrane
-
Zea mays
42651
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
Arabidopsis thaliana
More
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
Marchantia polymorpha
More
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
Nicotiana tabacum
More
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
Synechocystis sp.
More
NdhM, NdhO, and NdhL are NDH subunits specific to photosynthetic/cyanobacterial NDH
Zea mays
General Information
General Information
Commentary
Organism
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
Arabidopsis thaliana
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
Marchantia polymorpha
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
Nicotiana tabacum
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
Synechocystis sp.
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
Zea mays
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
Arabidopsis thaliana
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
Marchantia polymorpha
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
Nicotiana tabacum
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
Zea mays
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
Arabidopsis thaliana
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
Marchantia polymorpha
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
Nicotiana tabacum
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
Synechocystis sp.
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
Zea mays
General Information (protein specific)
General Information
Commentary
Organism
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
Arabidopsis thaliana
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
Marchantia polymorpha
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
Nicotiana tabacum
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
Synechocystis sp.
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
Zea mays
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
Arabidopsis thaliana
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
Marchantia polymorpha
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
Nicotiana tabacum
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
Zea mays
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
Arabidopsis thaliana
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
Marchantia polymorpha
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
Nicotiana tabacum
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
Synechocystis sp.
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
Zea mays
Other publictions for EC 1.6.99.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741964
Villegas
FAD binding properties of a c ...
Escherichia coli
Biochim. Biophys. Acta
1844
576-584
2014
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724488
Villegas
Maintenance and thermal stabil ...
Arabidopsis thaliana, Marchantia polymorpha, Nicotiana tabacum, Synechocystis sp., Zea mays
Biochimie
95
382-387
2013
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14
14
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746936
Lakhal
Oxygen uptake rates in the hy ...
Thermotoga maritima, Thermotoga maritima DSM 3109
Arch. Microbiol.
193
429-438
2011
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701758
Do
Engineering Escherichia coli f ...
Trichomonas vaginalis
Appl. Biochem. Biotechnol.
153
21-33
2009
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1
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6
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3
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7
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1
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4
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4
1
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3
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1
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6
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1
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4
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4
1
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3
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685693
Chakraborty
Two proteins with diaphorase a ...
Moorella thermoacetica
Biosci. Biotechnol. Biochem.
72
877-879
2008
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1
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2
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1
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692853
Platt
Proteomic, microarray, and sig ...
Pseudomonas aeruginosa
J. Bacteriol.
190
2739-2758
2008
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1
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1
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1
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4
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1
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677088
Kitazume
Involvement of Lys-308 in the ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) YN-1
Res. Microbiol.
157
956-959
2006
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2
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1
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658494
Shiraki
Involvement of glycine and asp ...
Bacillus sp. YN-1
Curr. Microbiol.
46
432-434
2003
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1
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5
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2
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392824
Marques
Activation of a NADH dehydroge ...
Homo sapiens
Biol. Signals
6
52-61
1997
1
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392825
Thiagalingam
-
Purification and characterizat ...
Bacillus megaterium
Can. J. Microbiol.
39
826-833
1993
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10
4
1
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1
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10
1
4
1
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5
1
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392819
Nisimoto
NADH dehydrogenase from bovine ...
Bos taurus
J. Biol. Chem.
261
285-290
1986
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3
2
2
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2
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1
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392812
Borneleit
-
Purification and properties of ...
Acinetobacter calcoaceticus
Biochim. Biophys. Acta
722
94-101
1983
1
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392820
Bergsma
Purification and characterizat ...
Bacillus subtilis, Bacillus subtilis W23
Eur. J. Biochem.
128
151-157
1982
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3
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1
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8
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1
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1
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1
1
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1
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392811
Kitajima
Purification and properties of ...
Homo sapiens
Arch. Biochem. Biophys.
210
330-339
1981
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7
2
1
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2
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1
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1
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1
1
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6
1
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1
2
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3
1
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3
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7
1
2
1
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2
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1
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1
1
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6
1
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1
2
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392810
Wang
Human erythrocyte NADH: (accep ...
Homo sapiens
Biochim. Biophys. Acta
616
22-29
1980
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3
2
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1
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1
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1
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1
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392805
Adachi
Study on the reduced pyridine ...
Bos taurus
Biochim. Biophys. Acta
268
629-637
1972
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1
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1
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1
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1
1
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1
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1
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1
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1
1
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2
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-
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-
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392821
Ramanarayanan
Purification & properties of a ...
Agrobacterium tumefaciens
Indian J. Biochem. Biophys.
8
214-218
1971
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1
1
1
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1
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1
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1
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3
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1
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4
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4
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1
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1
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1
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3
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1
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392807
Kaniuga
The Transformation of mitochon ...
Sus scrofa
Biochim. Biophys. Acta
73
550-564
1963
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2
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1
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1
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