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Literature summary for 1.18.1.2 extracted from

  • Teshima, K.; Fujita, S.; Hirose, S.; Nishiyama, D.; Kurisu, G.; Kusunoki, M.; Kimata-Ariga, Y.; Hase, T.
    A ferredoxin Arg-Glu pair important for efficient electron transfer between ferredoxin and ferredoxin-NADP(+) reductase (2003), FEBS Lett., 546, 189-194.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information construction of ferredoxin II mutants Q39R/S28E and D64N by site-directed mutagenesis, expression of recombinant wild-type and mutant ferredoxins of Equisetum arvense in Escherichia coli Equisetum arvense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Equisetum arvense
0.0017
-
oxidized ferredoxin II wild-type cofactor, pH 7.5, 25°C Equisetum arvense
0.0053
-
oxidized ferredoxin II mutant D64N pH 7.5, 25°C Equisetum arvense
0.0114
-
oxidized ferredoxin I wild-type cofactor, pH 7.5, 25°C Equisetum arvense
0.0115
-
oxidized ferredoxin II mutant Q39R/S28E pH 7.5, 25°C Equisetum arvense

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced ferredoxin + NADP+ Equisetum arvense
-
oxidized ferredoxin + NADPH
-
?

Organism

Organism UniProt Comment Textmining
Equisetum arvense
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxidized ferredoxin I + NADPH + H+
-
Equisetum arvense reduced ferredoxin I + NADP+
-
r
oxidized ferredoxin II + NADPH + H+
-
Equisetum arvense reduced ferredoxin II NADP+
-
r
oxidized ferredoxin II mutant D64N + NADPH + H+
-
Equisetum arvense reduced ferredoxin II mutant D64N + NADP+
-
r
oxidized ferredoxin II mutant Q39R/S28E + NADPH + H+
-
Equisetum arvense reduced ferredoxin mutant Q39R/S28E + NADP+
-
r
reduced ferredoxin + NADP+
-
Equisetum arvense oxidized ferredoxin + NADPH
-
?
reduced ferredoxin + NADP+ recombinant ferredoxin I and II, and ferredoxin I mutants, the Fd I Q39R/S28E mutant lacks the Arg39-Glu28 residues being essential for efficient electron transfer between the cofactor and the enzyme Equisetum arvense oxidized ferredoxin + NADPH
-
?
reduced ferredoxin I + NADP+
-
Equisetum arvense oxidized ferredoxin I + NADPH + H+
-
r
reduced ferredoxin II + NADP+
-
Equisetum arvense oxidized ferredoxin II + NADPH + H+
-
r

Synonyms

Synonyms Comment Organism
Fd-NADP+ reductase
-
Equisetum arvense
Ferredoxin-NADP(+) reductase
-
Equisetum arvense
FNR
-
Equisetum arvense

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Equisetum arvense

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
32.2
-
reduced ferredoxin II wild-type cofactor, pH 7.5, 25°C Equisetum arvense
36.8
-
reduced ferredoxin II ferredoxin mutant D64N pH 7.5, 25°C Equisetum arvense
147
-
reduced ferredoxin II ferredoxin mutant Q39R/S28E, pH 7.5, 25°C Equisetum arvense
177
-
reduced ferredoxin I wild-type cofactor, pH 7.5, 25°C Equisetum arvense

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Equisetum arvense

Cofactor

Cofactor Comment Organism Structure
Ferredoxin [2Fe2S] cluster containing, ferredoxin I and II, and ferredoxin I mutants, the latter lacking the Arg39-Glu28 residues being essential for efficient electron transfer between the cofactor and the enzyme, the Fd I Q39R/S28E mutant is unstable and rapidly loose the [2Fe2S] cluster, the mutant shows 5.5fold reduced electron transfer rates compared to Fd I, ferredoxin II mutant D64N is about half as efficient as cofactor as the wild-type ferredoxin I and II are Equisetum arvense