Information on EC 1.18.1.3 - ferredoxin-NAD+ reductase

2 ferricytochrome c + NADH

2 ferrocytochrome c + NAD+ + H+

2 reduced ferredoxin + NAD+ + H+

2 oxidized ferredoxin + NADH

ferredoxin + NADH

reduced ferredoxin + NAD+ + H+

ferricyanide + NADH

ferrocyanide + NAD+ + H+

-

Substrates: -
Products: -

?

ferricytochrome c + NADH

ferrocytochrome c + NAD+ + H+

flavodoxin hydroquinone + NADH

flavodoxin hydroquinol + NAD+ + H+

NADH + nitroblue tetrazolium

NAD+ + reduced nitroblue tetrazolium

-

Substrates: -
Products: -

?

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+

17 entries

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

?

-

8 entries

2 reduced ferredoxin + NAD+ + H+

2 oxidized ferredoxin + NADH

ferredoxin + NADH

reduced ferredoxin + NAD+ + H+

flavodoxin hydroquinone + NADH

flavodoxin hydroquinol + NAD+ + H+

oxidized ferredoxin + NADH

reduced ferredoxin + NAD+

9 entries

oxidized ferredoxin + NADPH

reduced ferredoxin + NADP+

Streptomyces coelicolor

-

658575

Substrates: enzyme enhances the level of the active form of CYP105D1
Products: -

?

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

?

-

FAD

9 entries

Ferredoxin

-

NAD+

NADH

NADPH

[2Fe-2S]-center

additional information

no activity with NADPH

-

Fe2+

-

in an iron-sulfur center

Iron

-

iron-sulfur flavoprotein, protein contains 1.8 gatom of iron and 2.0 gatom of acid-labile sulfur

Li+

-

required for activity

Mg2+

-

required

Na+

-

required for activity

1,10-phenanthroline

2,2'-dipyridyl

-

iodoacetate

-

10 mM, 50% inhibition

KCl

-

sharp decrease in activity in presence of up to 50 mM KCl, smaller increase in inhibition above

NaCl

-

sharp decrease in activity in presence of up to 50 mM KCl, smaller increase in inhibition above

NADH

NEM

-

10 mM, 67% inhibition

PCMB

Sodium azide

-

40 mM, 46% inhibition

acetyl Co-A

0.0046

ferricytochrome c

-

0.002

flavodoxin hydroquinone

-

at pH 6.8, temperature not specified in the publication

-

0.0105 - 0.125

NADH

0.156

NADPH

-

reaction with 2,6-dichlorophenolindophenol

0.0000037 - 0.0000105

oxidized ferredoxin

0.0014

oxidized [2Fe-2S] ferredoxin

-

at pH 6.8, temperature not specified in the publication

Methylosinus trichosporium OB3b

additional information

-

Km-values for transhydrogenase reaction

437844

-

60.2

ferricyanide

-

pH 8.5, 30°C

4.5

ferricytochrome c

-

pH 8.5, 30°C

Methylosinus trichosporium OB3b

0.75

-

12.3

-

397

-

50000

Acetobacterium woodii

-

substrate CO-reduced ferredoxin, pH 7.7, 30°C

727962

6.6 - 7.5

-

7

-

assay at

7.2

-

reduction of 2,6-dichlorophenolindophenol

8.4

-

8.8

-

25

-

assay at

32

-

reduction of 2,6-dichlorophenolindophenol

additional information

-

no activity detected at 5°C or at 55°C. Activity at 50°C is 15.2% of maximal activity

Acetivibrio thermocellus

-

437848

-

Acetobacterium woodii

-

727962

-

Acetobacterium woodii DSM 103

-

727962

-

-

Acidaminococcus fermentans DSM 20731

-

-

-

Pseudomonas sp., strain KKS102

-

-

-

Acinetobacter sp.

-

746345

-

-

Azotobacter vinelandii UW136

-

-

Clostridium acetobutylicum

-

-

437849, 437850

-

Clostridium butyricum

-

437843, 437851

-

Clostridium kluyveri

-

437843

-

Clostridium ljungdahlii

-

728235

D8GR70

UniProt

Clostridium ljungdahlii DSM 13528

-

728235

D8GR70

UniProt

Clostridium pasteurianum

-

437843, 437847, 437850, 437851

-

Clostridium tyrobutyricum

-

437847, 437850

-

Clostridium tyrobutyricum CNRZ 510

-

437847

-

Methylosinus trichosporium OB3b

-

437844

-

-

673520, 675830

-

-

-

-

-

carAd or fdr gene

-

Novosphingobium sp. KA1

carAd or fdr gene

Oleidesulfovibrio alaskensis

-

-

745970

-

Oleidesulfovibrio alaskensis G20

-

745970

-

enzyme acts as reductase subunit of p-cymene mono-oxygenase, EC 1.14.15.25

UniProt

Pseudomonas sp. LB400

-

Pseudomonas sp. NCIB 9816

-

-

-

-

Rhodopseudomonas palustris CGA009

-

-

Thermoanaerobacter brockii

-

Streptomyces coelicolor

two different isoforms

658575

-

-

437848

-

Thermoanaerobacter thermohydrosulfuricus

activity is present in wild-type strain, alcohol-adapted strain lacks detectable levels of reduced ferredoxin-linked NAD reductase

437845

-

[Butyribacterium] methylotrophicum

-

437854

-

membrane

11 entries

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

malfunction

physiological function

6 entries

additional information

12 entries

Ectopseudomonas mendocina

Marinomonas mediterranea MMB-1

Pseudomonas putida F1

34900

-

non-denaturing PAGE

36000

37000

-

gel filtration

39000

gel fitlration

39800

-

x * 39800, recombinant His-tagged RedIIA, SDS-PAGE

41500

-

NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase, gel filtration

42000

gel filtration

42396

-

1 * 42396, calculated, 1 * 50000, SDS-PAGE

43000

-

x * 69000, SDS-PAGE, GST-fusion protein, x * 43000, SDS-PAGE, native protein

43600

-

1 * 43600, NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase, SDS-PAGE

46000

-

1 * 46000, SDS-PAGE

46500

-

gel filtration

50000

-

gel filtration

69000

-

x * 69000, SDS-PAGE, GST-fusion protein, x * 43000, SDS-PAGE, native protein

?

monomer

8 entries

additional information

purified recombinant BphA4 in complex with BphA3, anaerobic crystallization is essential to crystallize the productive complex between oxidized BphA3 and NADH-reduced BphA4, sitting-drop vapour-diffusion method, 26.4 mg/ml BphA4 in 50 mM potassium phosphate buffer, pH 7.0, is reduced with 20 mM NADH for 5 min at 4°C, and mixed with oxidized BphA3 at a concentration of 17.5 mg/ml, mixing of 0.9 ml of each of the protein and reservoir solutions, and equilibration against 500 ml reservoir solution, containing 0.2 M ammonium acetate, 0.1 M sodium citrate, pH 5.6, 30% w/v PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 1.9 A resolution

-

recombinant His-tagged RedIIA from KA1, hanging-drop vapour-diffusion, 5°C, method using PEG 4000, X-ray diffraction structure determination and analysis at 1.58 A resolution, modelling

-

ferredoxin reductase component of biphenyl dioxygenase

-

437852

purified recombinant enzyme, hanging-drop vapour-diffusion method, 0.001 ml of protein solution with 20mg/ml protein in 20 mM HEPES, pH 7.0, and 0.001 ml reservoir solution, containing 100 mM HEPES, pH 7.0-7.2, 16-18% w/v PEG 10 000 at 18°C, are mixed and equilibrated against 200 ml reservoir solution, 70 mM sodium cacodylate pH 6.5, 0.98 M sodium acetate, 30% v/v glycerol are best for cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement using the putidaredoxin reductase structure, overview

-

additional information

0.5

-

5 d, 30% loss of activity

21

-

room temperature, 8 h, 50% loss of activity

30

10 min, 42% loss of activity

50

10 min, 98% loss of activity

-20°C, 1 month, minimal loss of activity

-

-20°C, 3 months, little loss of activity

-

0-4°C, stable for up to 30 h

-

0-5°C, 30% loss of activity after 5 days

-

70°C, 50 mM potassium phosphate buffer (pH 7.0), 60% glycerol (v/v), subunit CymA is stable for 1 month

-

Blue-sepharose column chromatography

-

electron-transfer component XylA

P21394

744831

NADH-ferredoxin oxidoreductase component of biphenyl 2,3-dioxygenase

-

NADH-ferredoxinNAP reductase component of naphthalene dioxygenase

-

recombinant BphA4 under aerobic conditions from Escherichia coli JM109 cells by anion exchange and adsorption chromatography, and ultrafiltration

-

recombinant enzyme from Escherichia col strain BL21(DE3) by repeated anion exchange chromatography, using a linear gradient of NaCl in 20 mM HEPES buffer, pH 7.0, for elution, followed by gel filtration and ultrafiltration

-

recombinant His-tagged RedIIA from Escherichia coli strain BL21(DE3) by metal affinity chromatography and gel filtration

-

recombinant protein

-

-

both isoforms expressed in Escherichia coli BL21 StarTM (DE3) and Streptomyces lividans together with CYP105D1 from Streptomyces griseus

Streptomyces coelicolor

-

658575

expressed in Escherichia coli JM109 cells

-

expressed in Escherichia coli MV1304 as GST-fusion protein

-

gene carAd or fdr, from genomic DNA, expression of His-tagged Red in Escherichia coli strain BL21(DE3)

-

gene rfn, the Azotobacter vinelandii genome contains two homologous rnf operons (deduced amino acid sequence identity of 30-48%, depending on the subunit), both encoding functional Rnf. Of them, rnf1 is induced under diazotrophic conditions, whereas the nf2 is expressed independently of the nitrogen source in the medium. The Rnf complexes are membrane-integral proteins formed by six subunits (RnfABCDEG), each encoded by a separate gene of the rnf operons

-

overexpression of BphA4 in Escherichia coli JM109 cells

-

overexpression of PuR in Escherichia coli strain BL21(DE3) using the tandem tac promoters in the pCWori+ vector

-

expression of subunits CymABM is induced by growth on p-cymene

reconstitution of P450-containing mono-oxygenase using purified homologous enzyme, ferrdoxin and P450

-