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2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
ferricyanide + NADH
ferrocyanide + NAD+ + H+
-
-
-
-
?
ferricytochrome c + NADH
ferrocytochrome c + NAD+ + H+
flavodoxin hydroquinone + NADH
flavodoxin hydroquinol + NAD+ + H+
NADH + nitroblue tetrazolium
NAD+ + reduced nitroblue tetrazolium
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenolindophenol + H+
NAD+ + reduced 2,6-dichlorophenolindophenol
NADH + oxidized nitro blue tetrazolium + H+
NAD+ + reduced nitro blue tetrazolium
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
NADPH + oxidized cytochrome c
NADP+ + reduced cytochrome c
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
reduced ferredoxin + NAD+
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
reduced [2Fe-2S] ferredoxin + NAD+ + H+
oxidized [2Fe-2S] ferredoxin + NADH
additional information
?
-
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
-
?
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
-
BphA3, a Rieske-type [2Fe-2S] ferredoxin, and BphA4 comprise an electron-transfer system for the multi-component dioxygenase BphA, BphA4 receives two electrons from NADH as a form of hydride and transfers an electron to each of two BphA3 molecules, molecular mechanism of the electron transfer between BphA3 and BphA4, overview
-
-
?
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
-
the enzyme is an essential component of the cytochrome P450 systems in Rhodopseudomonas palustris strain CGA009, a model organism with diverse metabolic pathways
-
-
?
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
-
electron transport is initiated by a single two-electron transfer from NAD(P)H to FAD to produce fully reduced FADH2, which provides one electron to the iron-sulfur cluster, in most cases a [2Fe2S] cluster, of ferredoxins. These electrons are finally transferred to the terminal oxygenase, mechanism of electron transport, overview
-
-
?
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
-
the enzyme is an essential component of the cytochrome P450 systems in Rhodopseudomonas palustris strain CGA009, a model organism with diverse metabolic pathways
-
-
?
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
-
electron transport is initiated by a single two-electron transfer from NAD(P)H to FAD to produce fully reduced FADH2, which provides one electron to the iron-sulfur cluster, in most cases a [2Fe2S] cluster, of ferredoxins. These electrons are finally transferred to the terminal oxygenase, mechanism of electron transport, overview
-
-
?
ferricytochrome c + NADH
ferrocytochrome c + NAD+ + H+
-
-
-
-
r
ferricytochrome c + NADH
ferrocytochrome c + NAD+ + H+
-
-
-
-
r
flavodoxin hydroquinone + NADH
flavodoxin hydroquinol + NAD+ + H+
-
-
-
-
ir
flavodoxin hydroquinone + NADH
flavodoxin hydroquinol + NAD+ + H+
-
-
-
-
ir
flavodoxin hydroquinone + NADH
flavodoxin hydroquinol + NAD+ + H+
-
-
-
-
ir
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 nitro blue tetrazolium + H+
NAD+ + reduced nitro blue tetrazolium
-
-
-
-
?
NADH + oxidized nitro blue tetrazolium + H+
NAD+ + reduced nitro blue tetrazolium
-
-
-
-
?
NADH + oxidized nitro blue tetrazolium + H+
NAD+ + reduced nitro blue tetrazolium
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + oxidized cytochrome c
NADP+ + reduced cytochrome c
-
39% of the activity with NADH
-
-
?
NADPH + oxidized cytochrome c
NADP+ + reduced cytochrome c
-
39% of the activity with NADH
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
-
-
-
r
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
essential step in glucose fermentation
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
catabolic enzyme
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
essential step in glucose fermentation
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
-
-
-
r
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
ferredoxin from Clostridium tyrobutyricum and Clostridium acetobutylicum
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
essential step in glucose fermentation
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
catabolic enzyme
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
-
-
-
r
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
ferredoxin from Clostridium tyrobutyricum and Clostridium acetobutylicum
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
ferredoxin from Clostridium tyrobutyricum and Clostridium acetobutylicum
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
the enzyme couples electron flow from formate dehydrogenase (NAD+ requiring) to ferredoxin
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
-
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
required for activity of CYP101
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
-
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
-
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
the enzyme is required for the mechanism of CO tolerance by the CO-adapted strain
-
-
?
oxidized ferredoxin + NADH + H+
reduced ferredoxin + NAD+
-
endergonic ferredoxin reduction with NADH as reductant is possible, but only in the presence of a membrane potential, and is accompanied by Na+ efflux out of the vesicles
-
-
r
oxidized ferredoxin + NADH + H+
reduced ferredoxin + NAD+
-
endergonic ferredoxin reduction with NADH as reductant is possible, but only in the presence of a membrane potential, and is accompanied by Na+ efflux out of the vesicles
-
-
r
oxidized ferredoxin + NADH + H+
reduced ferredoxin + NAD+
-
endergonic ferredoxin reduction with NADH as reductant is possible, but only in the presence of a membrane potential, and is accompanied by Na+ efflux out of the vesicles
-
-
r
oxidized ferredoxin + NADH + H+
reduced ferredoxin + NAD+
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
-
-
-
?
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
enzyme enhances the level of the active form of CYP105D1
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
-
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
-
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
-
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
-
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
-
-
-
?
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
-
ferredoxin is reduced with CO, catalyzed by the purified acetyl-CoA synthase/CO dehydrogenase. Using CO-reduced ferredoxin, NAD+ reduction is highly specific and strictly dependent on ferredoxin. Electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport, indicating the generation of a sodium ion potential. Vice versa, endergonic ferredoxin reduction with NADH as reductant is possible, but only in the presence of a sodium ion potential, and is accompanied by Na+ efflux out of the vesicles
-
-
r
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
-
ferredoxin is reduced with CO, catalyzed by the purified acetyl-CoA synthase/CO dehydrogenase. Using CO-reduced ferredoxin, NAD+ reduction is highly specific and strictly dependent on ferredoxin. Electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport, indicating the generation of a sodium ion potential. Vice versa, endergonic ferredoxin reduction with NADH as reductant is possible, but only in the presence of a sodium ion potential, and is accompanied by Na+ efflux out of the vesicles
-
-
r
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
-
ferredoxin is reduced with CO, catalyzed by the purified acetyl-CoA synthase/CO dehydrogenase. Using CO-reduced ferredoxin, NAD+ reduction is highly specific and strictly dependent on ferredoxin. Electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport, indicating the generation of a sodium ion potential. Vice versa, endergonic ferredoxin reduction with NADH as reductant is possible, but only in the presence of a sodium ion potential, and is accompanied by Na+ efflux out of the vesicles
-
-
r
reduced [2Fe-2S] ferredoxin + NAD+ + H+
oxidized [2Fe-2S] ferredoxin + NADH
-
-
-
-
?
reduced [2Fe-2S] ferredoxin + NAD+ + H+
oxidized [2Fe-2S] ferredoxin + NADH
Oleidesulfovibrio alaskensis
-
-
-
-
?
reduced [2Fe-2S] ferredoxin + NAD+ + H+
oxidized [2Fe-2S] ferredoxin + NADH
Oleidesulfovibrio alaskensis G20
-
-
-
-
?
additional information
?
-
-
the enzyme BphA4 is an FAD-containing NADHdependent ferredoxin reductase
-
-
?
additional information
?
-
-
the enzyme can, depending on cellular conditions, produce or oxidize NADH. NADH-ferredoxin reductase can control the level of NAD+ and NADH in the cell
-
-
?
additional information
?
-
-
the enzyme can, depending on cellular conditions, produce or oxidize NADH. NADH-ferredoxin reductase can control the level of NAD+ and NADH in the cell
-
-
?
additional information
?
-
-
the enzyme can, depending on cellular conditions, produce or oxidize NADH. NADH-ferredoxin reductase can control the level of NAD+ and NADH in the cell
-
-
?
additional information
?
-
-
the enzyme also has transhydrogenase activity which transfers electrons and protons from NADH to thionicotinamide adenine dinucleotide phosphate and from NADPH to acetylpyridine adenine dinucleotide
-
-
?
additional information
?
-
-
no substrates of enzyme: morpholine, piperidine, pyrrolidine. Morpholine is a substrate of the P450mor system, consisting of enzyme, Fe3S4 ferredoxin and cytochrome P450
-
-
?
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ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
flavodoxin hydroquinone + NADH
flavodoxin hydroquinol + NAD+ + H+
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
-
enzyme enhances the level of the active form of CYP105D1
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
reduced [2Fe-2S] ferredoxin + NAD+ + H+
oxidized [2Fe-2S] ferredoxin + NADH
additional information
?
-
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
-
BphA3, a Rieske-type [2Fe-2S] ferredoxin, and BphA4 comprise an electron-transfer system for the multi-component dioxygenase BphA, BphA4 receives two electrons from NADH as a form of hydride and transfers an electron to each of two BphA3 molecules, molecular mechanism of the electron transfer between BphA3 and BphA4, overview
-
-
?
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
-
the enzyme is an essential component of the cytochrome P450 systems in Rhodopseudomonas palustris strain CGA009, a model organism with diverse metabolic pathways
-
-
?
ferredoxin + NADH
reduced ferredoxin + NAD+ + H+
-
the enzyme is an essential component of the cytochrome P450 systems in Rhodopseudomonas palustris strain CGA009, a model organism with diverse metabolic pathways
-
-
?
flavodoxin hydroquinone + NADH
flavodoxin hydroquinol + NAD+ + H+
-
-
-
-
ir
flavodoxin hydroquinone + NADH
flavodoxin hydroquinol + NAD+ + H+
-
-
-
-
ir
flavodoxin hydroquinone + NADH
flavodoxin hydroquinol + NAD+ + H+
-
-
-
-
ir
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
essential step in glucose fermentation
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
catabolic enzyme
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
essential step in glucose fermentation
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
essential step in glucose fermentation
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
catabolic enzyme
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
the enzyme couples electron flow from formate dehydrogenase (NAD+ requiring) to ferredoxin
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
required for activity of CYP101
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
-
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
-
the enzyme is required for the mechanism of CO tolerance by the CO-adapted strain
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
-
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
-
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
-
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
-
-
-
?
oxidized [2Fe-2S] ferredoxin + NADH
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
-
-
-
?
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
-
ferredoxin is reduced with CO, catalyzed by the purified acetyl-CoA synthase/CO dehydrogenase. Using CO-reduced ferredoxin, NAD+ reduction is highly specific and strictly dependent on ferredoxin. Electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport, indicating the generation of a sodium ion potential. Vice versa, endergonic ferredoxin reduction with NADH as reductant is possible, but only in the presence of a sodium ion potential, and is accompanied by Na+ efflux out of the vesicles
-
-
r
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
-
ferredoxin is reduced with CO, catalyzed by the purified acetyl-CoA synthase/CO dehydrogenase. Using CO-reduced ferredoxin, NAD+ reduction is highly specific and strictly dependent on ferredoxin. Electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport, indicating the generation of a sodium ion potential. Vice versa, endergonic ferredoxin reduction with NADH as reductant is possible, but only in the presence of a sodium ion potential, and is accompanied by Na+ efflux out of the vesicles
-
-
r
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH + H+
-
ferredoxin is reduced with CO, catalyzed by the purified acetyl-CoA synthase/CO dehydrogenase. Using CO-reduced ferredoxin, NAD+ reduction is highly specific and strictly dependent on ferredoxin. Electron transport from reduced ferredoxin to NAD+ is coupled to electrogenic Na+ transport, indicating the generation of a sodium ion potential. Vice versa, endergonic ferredoxin reduction with NADH as reductant is possible, but only in the presence of a sodium ion potential, and is accompanied by Na+ efflux out of the vesicles
-
-
r
reduced [2Fe-2S] ferredoxin + NAD+ + H+
oxidized [2Fe-2S] ferredoxin + NADH
-
-
-
-
?
reduced [2Fe-2S] ferredoxin + NAD+ + H+
oxidized [2Fe-2S] ferredoxin + NADH
Oleidesulfovibrio alaskensis
-
-
-
-
?
reduced [2Fe-2S] ferredoxin + NAD+ + H+
oxidized [2Fe-2S] ferredoxin + NADH
Oleidesulfovibrio alaskensis G20
-
-
-
-
?
additional information
?
-
-
the enzyme can, depending on cellular conditions, produce or oxidize NADH. NADH-ferredoxin reductase can control the level of NAD+ and NADH in the cell
-
-
?
additional information
?
-
-
the enzyme can, depending on cellular conditions, produce or oxidize NADH. NADH-ferredoxin reductase can control the level of NAD+ and NADH in the cell
-
-
?
additional information
?
-
-
the enzyme can, depending on cellular conditions, produce or oxidize NADH. NADH-ferredoxin reductase can control the level of NAD+ and NADH in the cell
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Broadus, R.M.; Haddock, J.D.
Purification and characterization of the NADH:ferredoxinBPH oxidoreductase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400
Arch. Microbiol.
170
106-112
1998
Pseudomonas sp., Pseudomonas sp. LB400
brenda
Haigler, B.E.; Gibson, D.T.
Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816
J. Bacteriol.
172
457-464
1990
Pseudomonas sp., Pseudomonas sp. NCIB 9816
brenda
Jungermann, K.; Leimenstoll, G.; Rupprecht, E.; Thauer, R.K.
Demonstration of NADH-ferredoxin reductase in two saccharolytic Clostridia
Arch. Mikrobiol.
80
370-372
1971
Clostridium butyricum, Clostridium kluyveri, Clostridium pasteurianum
brenda
Chen, Y.P.; Yoch, D.C.
Isolation, characterization, and biological activity of ferredoxin-NAD+ reductase from the methane oxidizer Methylosinus trichosporium OB3b
J. Bacteriol.
171
5012-5016
1989
Methylosinus trichosporium OB3b
brenda
Lovitt, R.W.; Shen, G.J.; Zeikus, J.G.
Ethanol production by thermophilic bacteria: biochemical basis for ethanol and hydrogen tolerance in Clostridium thermohydrosulfuricum
J. Bacteriol.
170
2809-2815
1988
Thermoanaerobacter thermohydrosulfuricus
brenda
Subramanian, V.; Liu, T.N.; Yeh, W.K.; Narro, M.; Gibson, D.T.
Purification and properties of NADH-ferredoxinTOL reductase. A component of toluene dioxygenase from Pseudomonas putida
J. Biol. Chem.
256
2723-2730
1981
Pseudomonas putida
brenda
Blusson, H.; Petitdemange, H.; Gay, R.
A new, fast, and sensitive assay for NADH-ferredoxin oxidoreductase detection in clostridia
Anal. Biochem.
110
176-181
1981
Clostridium pasteurianum, Clostridium tyrobutyricum, Clostridium tyrobutyricum CNRZ 510
brenda
Lamed, R.; Zeikus, J.G.
Ethanol production by thermophilic bacteria: relationship between fermentation product yields of and catabolic enzyme activities in Clostridium thermocellum and Thermoanaerobium brockii
J. Bacteriol.
144
569-578
1980
Thermoanaerobacter brockii, Acetivibrio thermocellus
brenda
Petitdemange, H.; Cherrier, C.; Bengone, J.M.; Gay, R.
Study of the NADH and NADPH-ferredoxin oxidoreductase activities in Clostridium acetobutylicum
Can. J. Microbiol.
23
152-160
1977
Clostridium acetobutylicum
brenda
Petitdemange, H.; Cherrier, C.; Raval, G.; Gay, R.
Regulation of the NADH and NADPH-ferredoxin oxidoreductases in clostridia of the butyric group
Biochim. Biophys. Acta
421
334-347
1976
Clostridium acetobutylicum, Clostridium pasteurianum, Clostridium tyrobutyricum
brenda
Jungermann, K.; Thauer, R.K.; Leimenstoll, G.; Decker, K.
Function of reduced pyridine nucleotide-ferredoxin oxidoreductases in saccharolytic Clostridia
Biochim. Biophys. Acta
305
268-280
1973
Clostridium butyricum, Clostridium pasteurianum
brenda
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