1.19.1.1: flavodoxin-NADP+ reductase
This is an abbreviated version!
For detailed information about flavodoxin-NADP+ reductase, go to the full flat file.
Reaction
Synonyms
Bc_0385, ferredoxin (flavodoxin):NADP+ oxidoreductase, ferredoxin/flavodoxin-NADP(H) oxidoreductase, FLDR, FNR, FPR, PETH, YumC
ECTree
1.19.1.1 flavodoxin-NADP+ reductaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.19.1.1 - flavodoxin-NADP+ reductase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ferricytochrome c + NADPH + H+
2 ferrocytochrome c + NADP+ + H+
-
-
-
?
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
?
reduced 2,6-dichlorophenolindophenol + NADP+
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
-
-
-
?
reduced flavodoxin I + NADP+
oxidized flavodoxin I + NADPH + H+
-
-
-
?
reduced flavodoxin II + NADP+
oxidized flavodoxin II + NADPH + H+
-
-
-
?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+ + H+
-
-
-
?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
-
-
-
-
?
oxidized cytochrome c + NADH + H+
reduced cytochrome c + NAD+
-
-
-
-
r
oxidized cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH + H+
-
-
-
?
additional information
?
-
the enzyme reduces flavodoxin I, flavodoxin II and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner, i.e. reaction of EC 1.18.2.1. Flavodoxin I and flavodoxin II behave similarly with respect to FNR, with affinities about 4- to 7fold weaker and reduction rates that are 10- to 100fold slower than those for ferredoxin. Flavodoxin I and flavodoxin II can obtain electrons from reduced Fd at rates that are comparable to those obtained with reduced FNR
-
-
?
additional information
?
-
-
substrate flavodoxin is more structured when the FMN cofactor is bound. Holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase, whereas there is no detectable interaction between apo-flavodoxin and the protein
-
-
?
additional information
?
-
-
the electron-transfer route is NADPH to FLDR to flavodoxin. The midpoint reduction potentials of the oxidized/semiquinone and semiquinone/hydroquinone couples of FLDR are 2308 mV and 2268 mV, respectively. Binding of 2'-adenosine monophosphate increases the midpoint reduction potentials for both FLDR couples
-
-
?
additional information
?
-
Escherichia coli B / ATCC 11303
-
substrate flavodoxin is more structured when the FMN cofactor is bound. Holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase, whereas there is no detectable interaction between apo-flavodoxin and the protein
-
-
?
additional information
?
-
-
the electron-transfer route is NADPH to FLDR to flavodoxin. The midpoint reduction potentials of the oxidized/semiquinone and semiquinone/hydroquinone couples of FLDR are 2308 mV and 2268 mV, respectively. Binding of 2'-adenosine monophosphate increases the midpoint reduction potentials for both FLDR couples
-
-
?
additional information
?
-
no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein. The observed rate constants for reoxidation of ferredoxin by FNR (reaction of EC 1.18.1.2) are about 100fold decreased when phenylglyoxal-modified FNR is used. When phenylglyoxal-modified FNR is used to reduce flavodoxin, similar inhibitory effects are observed. In this case, the limiting first-order rate constant for flavodoxin semiquinone formation via intracomplex electron transfer is approximately 12fold smaller than that obtained for the native FNR. Ionic strength effects are diminished. Complex formation can still occur between modified FNR and native flavodoxin, and between native FNR and modified flavodoxin, but the geometry of these complexes is altered so as to decrease the effectiveness of interprotein electron transfer
-
-
?
additional information
?
-
no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein. The observed rate constants for reoxidation of ferredoxin by FNR (reaction of EC 1.18.1.2) are about 100fold decreased when phenylglyoxal-modified FNR is used. When phenylglyoxal-modified FNR is used to reduce flavodoxin, similar inhibitory effects are observed. In this case, the limiting first-order rate constant for flavodoxin semiquinone formation via intracomplex electron transfer is approximately 12fold smaller than that obtained for the native FNR. Ionic strength effects are diminished. Complex formation can still occur between modified FNR and native flavodoxin, and between native FNR and modified flavodoxin, but the geometry of these complexes is altered so as to decrease the effectiveness of interprotein electron transfer
-
-
?
additional information
?
-
enzyme additionally shows diaphorase activity which is induced by treatment with methyl viologen
-
-
?
additional information
?
-
-
enzyme additionally shows diaphorase activity which is induced by treatment with methyl viologen
-
-
?
