BRENDA - Enzyme Database show
show all sequences of 1.18.1.3

Function of reduced pyridine nucleotide-ferredoxin oxidoreductases in saccharolytic Clostridia

Jungermann, K.; Thauer, R.K.; Leimenstoll, G.; Decker, K.; Biochim. Biophys. Acta 305, 268-280 (1973)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
oxidized ferredoxin + NADH
Clostridium pasteurianum
catabolic enzyme
reduced ferredoxin + NAD+
-
-
?
oxidized ferredoxin + NADH
Clostridium butyricum
catabolic enzyme
reduced ferredoxin + NAD+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Clostridium butyricum
-
-
-
Clostridium pasteurianum
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
oxidized ferredoxin + NADH
catabolic enzyme
437851
Clostridium pasteurianum
reduced ferredoxin + NAD+
-
-
-
?
oxidized ferredoxin + NADH
catabolic enzyme
437851
Clostridium butyricum
reduced ferredoxin + NAD+
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Clostridium butyricum
NADH
-
Clostridium pasteurianum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Clostridium butyricum
NADH
-
Clostridium pasteurianum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
oxidized ferredoxin + NADH
Clostridium pasteurianum
catabolic enzyme
reduced ferredoxin + NAD+
-
-
?
oxidized ferredoxin + NADH
Clostridium butyricum
catabolic enzyme
reduced ferredoxin + NAD+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
oxidized ferredoxin + NADH
catabolic enzyme
437851
Clostridium pasteurianum
reduced ferredoxin + NAD+
-
-
-
?
oxidized ferredoxin + NADH
catabolic enzyme
437851
Clostridium butyricum
reduced ferredoxin + NAD+
-
-
-
?
Other publictions for EC 1.18.1.3
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)
746345
Ke
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Characterization of a novel C ...
Acinetobacter sp., Nocardia farcinica
Process Biochem.
62
59-68
2017
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745340
Chowdhury
Reduction of flavodoxin by el ...
Acidaminococcus fermentans, Acidaminococcus fermentans DSM 20731
J. Biol. Chem.
291
11993-12002
2016
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745970
Wang
The role of Rnf in ion gradie ...
Desulfovibrio alaskensis, Desulfovibrio alaskensis G20
PeerJ
4
e1919
2016
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1
1
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-
744269
Nishizawa
Complete pyridine-nucleotide- ...
Acidovorax sp. KKS102
Biochem. J.
462
257-265
2014
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1
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727962
Hess
The ferredoxin: NAD+ oxidoredu ...
Acetobacterium woodii, Acetobacterium woodii DSM 103
J. Biol. Chem.
288
31496-31502
2013
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1
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6
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728235
Tremblay
The Rnf complex of Clostridium ...
Clostridium ljungdahlii, Clostridium ljungdahlii DSM 13528
mBio
4
e00406
2012
-
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4
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1
1
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746333
Dutta
-
Purification and properties o ...
Pseudomonas chlororaphis subsp. aureofaciens
Process Biochem.
47
1263-1267
2012
-
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1
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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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2
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1
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1
-
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1
-
-
706994
Umeda
Crystallization and preliminar ...
Novosphingobium sp., Novosphingobium sp. KA1
Acta Crystallogr. Sect. F
66
712-714
2010
-
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1
1
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1
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3
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1
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1
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1
1
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684177
Peng
Crystallization and preliminar ...
Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009
Acta Crystallogr. Sect. F
63
422-425
2007
-
-
1
1
-
-
-
-
-
1
-
2
-
11
-
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1
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4
1
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2
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1
2
1
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1
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4
1
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684179
Senda
Crystallization and preliminar ...
Acidovorax sp.
Acta Crystallogr. Sect. F
63
520-523
2007
-
-
1
1
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-
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1
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2
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1
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2
1
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1
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1
1
1
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2
1
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658218
Zanno
MT FdR: a ferredoxin reductase ...
Mycobacterium tuberculosis
Biochim. Biophys. Acta
1707
157-169
2005
-
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1
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2
1
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1
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673520
Sielaff
Kinetic and binding studies wi ...
Mycobacterium sp., Mycobacterium sp. HE5
FEBS J.
272
1148-1159
2005
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2
3
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6
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6
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675830
Sielaff
Analysis of the nearly identic ...
Mycobacterium sp., Mycobacterium sp. HE5
Microbiology
151
2593-2603
2005
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2
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3
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4
2
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2
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1
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4
2
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2
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658575
Hussain
-
Ferredoxin reductase enhances ...
Streptomyces coelicolor
ENZYME MICROB. TECHNOL.
32
790-800
2003
-
-
1
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2
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1
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1
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2
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437852
Senda
Crystal structure of NADH-depe ...
Pseudomonas sp.
J. Mol. Biol.
304
397-410
2000
-
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1
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5
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437854
Shen
-
Biochemical basis for carbon m ...
Butyribacterium methylotrophicum
Appl. Microbiol. Biotechnol.
51
827-832
1999
-
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1
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1
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285290
Broadus
Purification and characterizat ...
Pseudomonas sp., Pseudomonas sp. LB400
Arch. Microbiol.
170
106-112
1998
-
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2
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2
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11
-
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1
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9
1
1
1
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1
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3
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3
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2
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2
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1
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9
1
1
1
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1
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744831
Shaw
Purification and characterisa ...
Pseudomonas putida
Eur. J. Biochem.
209
51-61
1992
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1
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1
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3
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3
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1
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1
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745194
Suzuki
Primary structure of xylene m ...
Pseudomonas putida
J. Bacteriol.
173
1690-1695
1991
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1
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437842
Haigler
Purification and properties of ...
Pseudomonas sp., Pseudomonas sp. NCIB 9816
J. Bacteriol.
172
457-464
1990
-
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5
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1
3
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6
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1
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1
2
10
1
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2
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3
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3
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5
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3
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1
2
10
1
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2
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437844
Chen
Isolation, characterization, a ...
Methylosinus trichosporium OB3b
J. Bacteriol.
171
5012-5016
1989
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2
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1
1
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7
-
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1
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1
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2
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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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2
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437845
Lovitt
Ethanol production by thermoph ...
Thermoanaerobacter thermohydrosulfuricus
J. Bacteriol.
170
2809-2815
1988
-
-
-
-
-
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-
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3
-
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437846
Subramanian
Purification and properties of ...
Pseudomonas putida
J. Biol. Chem.
256
2723-2730
1981
-
-
-
-
-
-
3
2
-
-
2
-
-
1
-
-
1
-
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-
1
2
5
1
-
-
-
-
1
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2
-
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2
-
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-
3
-
2
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-
2
-
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1
-
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1
2
5
1
-
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-
1
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-
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-
-
-
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-
-
437847
Blusson
A new, fast, and sensitive ass ...
Clostridium pasteurianum, Clostridium tyrobutyricum, Clostridium tyrobutyricum CNRZ 510
Anal. Biochem.
110
176-181
1981
-
-
-
-
-
-
-
-
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-
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3
-
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3
-
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2
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2
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3
-
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437848
Lamed
Ethanol production by thermoph ...
Hungateiclostridium thermocellum, Thermoanaerobacter brockii
J. Bacteriol.
144
569-578
1980
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437849
Petitdemange
Study of the NADH and NADPH-fe ...
Clostridium acetobutylicum
Can. J. Microbiol.
23
152-160
1977
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1
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437850
Petitdemange
Regulation of the NADH and NAD ...
Clostridium acetobutylicum, Clostridium pasteurianum, Clostridium tyrobutyricum
Biochim. Biophys. Acta
421
334-347
1976
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6
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6
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437851
Jungermann
Function of reduced pyridine n ...
Clostridium butyricum, Clostridium pasteurianum
Biochim. Biophys. Acta
305
268-280
1973
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2
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2
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2
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2
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437843
Jungermann
Demonstration of NADH-ferredox ...
Clostridium butyricum, Clostridium kluyveri, Clostridium pasteurianum
Arch. Mikrobiol.
80
370-372
1971
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3
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4
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