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Literature summary for 1.14.12.12 extracted from

  • Haigler, B.E.; Gibson, D.T.
    Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816 (1990), J. Bacteriol., 172, 457-464.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.12.12

Activating Compound

Activating Compound Comment Organism Structure
ferricyanide activation, direct reduction by reductaseNAP in the presence of NADH in vitro Pseudomonas sp.

General Stability

General Stability Organism
purification of reductase leads to significant loss of flavin cofactor Pseudomonas sp.

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline 10 mM, 63% inhibition of ferredoxinNAP reductase Pseudomonas sp.
4-chloromercuribenzoate 0.0005 mM, 94% inhibition of ferredoxinNAP reductase Pseudomonas sp.
iodoacetate 10 mM, 50% inhibition of ferredoxinNAP reductase Pseudomonas sp.
N-ethylmaleimide 2 mM, 30% inhibition of ferredoxinNAP reductase Pseudomonas sp.
NaN3 40 mM, 46% inhibition of ferredoxinNAP reductase Pseudomonas sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Pseudomonas sp. 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ component A, i.e. NADH-ferredoxinNAP reductase, of the multienzyme system is an iron-containing flavoprotein containing 1.8 g-atoms Fe2+ and 2 g-atoms sulfur Pseudomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 three component enzyme system consisting of: component A, i.e. ferredoxinNAP reductase, component B, i.e. terminal oxygenase ISPNAP, and component C, i.e. ferredoxinNAP Pseudomonas sp.
34900
-
 ferredoxinNAP reductase, native PAGE Pseudomonas sp.
36000
-
 1 * 36000, ferredoxinNAP reductase, SDS-PAGE Pseudomonas sp.
37000
-
 ferredoxinNAP reductase, gel filtration Pseudomonas sp.
37100
-
 ferredoxinNAP reductase, deduced from amino acid sequence Pseudomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
naphthalene + NADH + O2 Pseudomonas sp. three-component dioxygenase, uses two proteins containing three redox centers to transfer electrons to the terminal oxygenase (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ferredoxinNAP reductase, Blue Sepharose, DEAE-cellulose Pseudomonas sp.

Reaction

Reaction Comment Organism Reaction ID
naphthalene + NADH + H+ + O2 = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+ proposed electron transport chain: NADH, ferredoxixinNAP reductase, ferredoxinNAP, terminal oxygenase ISPNAP Pseudomonas sp.
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
397
-
 cytochrome c reduction by ferredoxinNAP reductase Pseudomonas sp.

Storage Stability

Storage Stability Organism
-20°C, ferredoxinNAP reductase, 1 month, minimal loss of activity, prolonged storage leads to precipitation when preparation is heated above 5°C Pseudomonas sp.
0-5°C, ferredoxinNAP reductase, 5 days, 30% loss of activity Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
naphthalene + NADH + O2 3 component enzyme system consisting of ferredoxinNAP reductase, ferredoxinNAP and oxygenase ISPNAP, ferredoxinNAP reductase reduces: 2,6-dichlorophenolindophenol, ferricyanide, nitro blue tetrazolium and cytochrome c, in the presence of FAD ferredoxinNAP reductase transfers electrons to ferredoxin Pseudomonas sp. cis-(1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
 ?
naphthalene + NADH + O2 three-component dioxygenase, uses two proteins containing three redox centers to transfer electrons to the terminal oxygenase Pseudomonas sp. (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD+
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 36000, ferredoxinNAP reductase, SDS-PAGE Pseudomonas sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
 room temperature, ferredoxinNAP reductase, t1/2: 8 h Pseudomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 ferredoxin reductaseNAP, pI: 6.3 Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
FAD 1 mol FAD/mol enzyme in flavin-reconstituted protein Pseudomonas sp.
FAD component A, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD Pseudomonas sp.
FAD addition enhances ferredoxinNAP reductase activity with all in vitro electron-acceptors, e.g. cytochrome c, 2,6-dichlorophenolindophenol, Nitroblue tetrazolium and ferricyanide Pseudomonas sp.
FMN requirement, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD, addition stimulates dioxygenase activity by 53% of FAD-stimulation Pseudomonas sp.
NADH
-
 Pseudomonas sp.
NADPH ferredoxinNAP reductase Pseudomonas sp.
NADPH can replace NADH with 39% Pseudomonas sp.