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Literature summary extracted from

  • Sato, J.; Takeda, K.; Nishiyama, R.; Watanabe, T.; Abo, M.; Yoshimura, E.; Nakagawa, J.; Abe, A.; Kawasaki, S.; Niimura, Y.
    Synechocystis ferredoxin-NADP+ oxidoreductase is capable of functioning as ferric reductase and of driving the Fenton reaction in the absence or presence of free flavin (2011), Biometals, 24, 311-321.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.16.1.9 flavin the enzyme is able to reduce iron compounds in the absence of free flavin, but the ferric reduction by the enzyme is enhanced by the addition of free flavin n the presence of natural chelate iron compounds but also synthetic chelate iron compounds Synechocystis sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.16.1.9 expressed in Escherichia coli strain JM109 Synechocystis sp.
1.18.1.2 expression in Escherichia coli Synechocystis sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.16.1.9 0.0168
-
 Fe(III)-EDTA in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.16.1.9 0.0276
-
 Fe(III)-citrate in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.16.1.9 0.16
-
 Fe(III)-citrate in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.16.1.9 0.5762
-
 Fe(III)-EDTA in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.16.1.9 34000
-
 2 * 34000, SDS-PAGE Synechocystis sp.
1.16.1.9 60000
-
 gel filtration Synechocystis sp.
1.18.1.2 34000
-
 2 * 34000, SDS-PAGE Synechocystis sp.
1.18.1.2 60000
-
 gel filtration Synechocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.16.1.9 2 Fe(II)-siderophore + NADP+ + H+ Synechocystis sp.
-
 2 Fe(III)-siderophore + NADPH
-
 ?
1.16.1.9 additional information Synechocystis sp. DNA degradation occurring in the presence of NADPH, Fe(III)-EDTA and hydrogen peroxide is potently enhanced by the purified enzyme, indicating that the enzyme may drive the Fenton reaction, reducing ferric iron to ferrous iron when it evokes the Fenton reaction ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.16.1.9 Synechocystis sp.
-
-
-
1.18.1.2 Synechocystis sp. Q55318
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.16.1.9 ammonium sulfate precipitation, butyl Toyopearl column chromatography, DEAE Sepharose column chromatography, POROS HQ-H column chromatography, and Red Sepharose column chromatography Synechocystis sp.
1.16.1.9 native enzyme Synechocystis sp.
1.18.1.2
-
 Synechocystis sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.16.1.9 0.02
-
 crude extract, using tert-butyl hydroperoxide as substrate, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.16.1.9 0.91
-
 after 45.5fold purification, using tert-butyl hydroperoxide as substrate, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.18.1.2 0.31
-
 substrate Fe(III)-EDTA, pH 7.0, 25°C Synechocystis sp.
1.18.1.2 0.39
-
 substrate ferricytochrome c, pH 7.0, 25°C Synechocystis sp.
1.18.1.2 5.92
-
 substrate FMN, pH 7.0, 25°C Synechocystis sp.
1.18.1.2 6
-
 substrate FAD, pH 7.0, 25°C Synechocystis sp.
1.18.1.2 35.27
-
 substrate 2,6-dichlorophenolindophenol, pH 7.0, 25°C Synechocystis sp.
1.18.1.2 35.28
-
 substrate ferricyanide, pH 7.0, 25°C Synechocystis sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.16.1.9 2 Fe(II) + NADP+ + H+
-
 Synechocystis sp. 2 Fe(III) + NADPH
-
 ?
1.16.1.9 2 Fe(II)-cytochrome c + NADP+ + H+
-
 Synechocystis sp. 2 Fe(III)-cytochrome c + NADPH
-
 ?
1.16.1.9 2 Fe(II)-siderophore + NADP+ + H+
-
 Synechocystis sp. 2 Fe(III)-siderophore + NADPH
-
 ?
1.16.1.9 2 ferricyanide + NADPH
-
 Synechocystis sp. 2 ferrocyanide + NADP+ + H+
-
 ?
1.16.1.9 2 ferrocyanide + NADP+ + H+
-
 Synechocystis sp. 2 ferricyanide + NADPH
-
 ?
1.16.1.9 2,6-dichloroindophenol + NADPH + H+ best substrate in the presence and absence of FAD Synechocystis sp. ?
-
 ?
1.16.1.9 cytochrome c + NADPH + H+
-
 Synechocystis sp. ?
-
 ?
1.16.1.9 Fe(III)-citrate + NADPH + H+
-
 Synechocystis sp. ?
-
 ?
1.16.1.9 Fe(III)-deferoxamine + NADPH + H+
-
 Synechocystis sp. ?
-
 ?
1.16.1.9 Fe(III)-diethylenetriamine-N,N,N',N'',N''-pentaacetate + NADPH + H+
-
 Synechocystis sp. Fe(II) + diethylenetriamine-N,N,N',N'',N''-pentaacetate + NADP+ + H+
-
 ?
1.16.1.9 Fe(III)-EDTA + NADPH + H+
-
 Synechocystis sp. Fe(II) + EDTA + NADP+ + H+
-
 ?
1.16.1.9 Fe(III)-ferrichrome + NADPH + H+
-
 Synechocystis sp. ?
-
 ?
1.16.1.9 Fe(III)-nitrilotriacetic acid + NADPH + H+
-
 Synechocystis sp. ?
-
 ?
1.16.1.9 ferric ammonium citrate + NADPH + H+
-
 Synechocystis sp. ?
-
 ?
1.16.1.9 ferritin + NADPH + H+
-
 Synechocystis sp. ?
-
 ?
1.16.1.9 additional information no activity with NADH. In the absence of FAD, the enzyme shows no activity towards ferric citrate, Fe(III)-ferrichrome, Fe(III)-deferoxamine, Fe(III)-nitrilotriacetic acid, and transferrin Synechocystis sp. ?
-
 ?
1.16.1.9 additional information DNA degradation occurring in the presence of NADPH, Fe(III)-EDTA and hydrogen peroxide is potently enhanced by the purified enzyme, indicating that the enzyme may drive the Fenton reaction, reducing ferric iron to ferrous iron when it evokes the Fenton reaction Synechocystis sp. ?
-
 ?
1.16.1.9 additional information the purified enzyme reacts with cytochrome c, ferricyanide and 2,6-dichloroindophenol, the flavin-independent NADPH oxidoreductase elicites NADPH oxidation activity during reduction of t-butyl hydroperoxide in the presence of Fe(III)-EDTA Synechocystis sp. ?
-
 ?
1.16.1.9 tert-butyl hydroperoxide + NADPH + H+
-
 Synechocystis sp. ?
-
 ?
1.16.1.9 transferrin + NADPH + H+
-
 Synechocystis sp. ?
-
 ?
1.18.1.2 2 ferricyanide + NADPH
-
 Synechocystis sp. 2 ferrocyanide + NADP+ + H+
-
 ?
1.18.1.2 2 ferricytochrome c2 + NADPH
-
 Synechocystis sp. 2 ferrocytochrome c2 + NADP+ + H+
-
 ?
1.18.1.2 FAD + NADPH + H+
-
 Synechocystis sp. reduced FAD + NADP+
-
 ?
1.18.1.2 Fe(III)-EDTA + NADPH + H+
-
 Synechocystis sp. Fe(II) + EDTA + NADP+
-
 ?
1.18.1.2 FMN + NADPH + H+
-
 Synechocystis sp. reduced FMN + NADP+
-
 ?
1.18.1.2 additional information DNA degradation occurring in the presence of NADPH, Fe(III)-EDTA and hydrogen peroxide is potently enhanced by the purified enzyme. The enzyme is capable of functioning as ferric reductase and of driving the Fenton reaction in the absence or presence of free flavin Synechocystis sp. ?
-
 ?
1.18.1.2 oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
 Synechocystis sp. reduced 2,6-dichlorophenolindophenol + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.16.1.9 homodimer 2 * 34000, SDS-PAGE Synechocystis sp.
1.18.1.2 dimer 2 * 34000, SDS-PAGE Synechocystis sp.

Synonyms

EC Number Synonyms Comment Organism
1.16.1.9 ferredoxin-NADP(+) oxidoreductase
-
 Synechocystis sp.
1.16.1.9 ferredoxin-NADP+ oxidoreductase
-
 Synechocystis sp.
1.16.1.9 FNR(S)
-
 Synechocystis sp.
1.16.1.9 FNRS
-
 Synechocystis sp.
1.18.1.2 FNRS
-
 Synechocystis sp.
1.18.1.2 PETH
-
 Synechocystis sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.16.1.9 0.24
-
 Fe(III)-citrate in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.16.1.9 0.95
-
 Fe(III)-EDTA in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.16.1.9 1.11
-
 Fe(III)-citrate in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.16.1.9 2
-
 Fe(III)-EDTA in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.16.1.9 additional information the enzyme is flavin-independent Synechocystis sp.
1.16.1.9 NADPH
-
 Synechocystis sp.
1.18.1.2 FAD and FMN, ratio of FAD to FMN is 7.5 to 1 Synechocystis sp.
1.18.1.2 FMN and FAD, ratio of FAD to FMN is 7.5 to 1 Synechocystis sp.

General Information

EC Number General Information Comment Organism
1.16.1.9 metabolism the enzyme is driving the Fenton reaction Synechocystis sp.

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.16.1.9 0.12
-
 Fe(III)-EDTA in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.16.1.9 1.59
-
 Fe(III)-citrate in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.16.1.9 41
-
 Fe(III)-citrate in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.
1.16.1.9 122
-
 Fe(III)-EDTA in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C Synechocystis sp.