Literature summary for 1.18.1.2 extracted from

Carrillo, N.; Ceccarelli, E.A.
Open questions in ferredoxin-NADP+ reductase catalytic mechanism (2003), Eur. J. Biochem., 270, 1900-1915.

Activating Compound

Activating Compound	Comment	Organism
flavodoxin	stimulates about 2fold the reduction of NADP+	Escherichia coli
additional information	acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Spinacia oleracea
additional information	acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Zea mays
additional information	acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Capsicum annuum
additional information	acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Pisum sativum
additional information	acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Cyanobacteria
additional information	acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Zea mays
NADP+	stimulates binding of reduced ferredoxin and reduction of flavin	Spinacia oleracea

Protein Variants

Protein Variants	Comment	Organism
additional information	a tyrosine mutant accepts NAD(H) as cofactor and is insensitive to inhibition by NADH	Spinacia oleracea
Y308S	altered cofactor specificity compared to the wild-type enzyme, mutant enzymes is able to utilizes NADP(H) as well as NAD(H)	Pisum sativum

Inhibitors

Inhibitors	Comment	Organism
Dithionite	-	Escherichia coli
NADH	-	Spinacia oleracea
NADPH	reversible inhibition, is turned to irreversible in presence of 4 M urea	Spinacia oleracea
oxidized ferredoxin	inhibits binding of reduced ferredoxin and reduction of flavin	Spinacia oleracea

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
additional information	-	additional information	kinetics	Escherichia coli
additional information	-	additional information	kinetics	Spinacia oleracea
additional information	-	additional information	kinetics	Anabaena sp.

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast	-	Spinacia oleracea	9507	-
chloroplast	-	Pisum sativum	9507	-
chloroplast	-	Zea mays	9507	-
chloroplast	-	Capsicum annuum	9507	-
chloroplast	-	Cyanobacteria	9507	-
plastid	-	Zea mays	9536	-
thylakoid	-	Pisum sativum	9579	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	enzyme contains an [2Fe2S] cluster as prosthetic group involved in the reaction	Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
reduced ferredoxin + NADP+	Rhodobacter capsulatus	-	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	Azotobacter vinelandii	-	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	Anabaena sp.	-	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	Spinacia oleracea	enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	Pisum sativum	enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	Zea mays	enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	Capsicum annuum	enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	Cyanobacteria	enzyme catalyzes the final step of photosynthetic electron transfer fron the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation, enzyme is involved in dinitrogen fixation in heterocysts	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	Escherichia coli	enzyme is involved in protection against oxidative stress, and in activation of anaerobic enzymes	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	Zea mays	in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction, reaction is part of nitrogen assimilation in nonphotosynthetic tissues	oxidized ferredoxin + NADPH	-	r

Organism

Organism	UniProt	Comment	Textmining
Anabaena sp.	-	-	-
Azotobacter vinelandii	-	-	-
Capsicum annuum	-	-	-
Cyanobacteria	-	-	-
Escherichia coli	-	-	-
Pisum sativum	-	-	-
Rhodobacter capsulatus	-	-	-
Spinacia oleracea	-	-	-
Zea mays	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH	reaction mechanism	Rhodobacter capsulatus	a
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH	reaction mechanism	Azotobacter vinelandii	a
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH	active site structure, reaction mechanism	Pisum sativum	a
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH	active site structure, reaction mechanism	Zea mays	a
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH	active site structure, reaction mechanism	Capsicum annuum	a
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH	active site structure of the plant-type enzyme, reaction mechanism	Cyanobacteria	a
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH	active site structure, ping pong reaction mechanism	Spinacia oleracea	a
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH	reaction mechanism, interaction and electron transfer	Anabaena sp.	a
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH	reaction mechanism, substrate recognition mechanism	Escherichia coli	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
heterocyst	-	Cyanobacteria	-
leaf	-	Spinacia oleracea	-
leaf	-	Zea mays	-
root	-	Zea mays	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2 ferricyanide + NADPH	diaphorase reaction	Escherichia coli	2 ferrocyanide + NADP+ + H+	-	?
2 ferricyanide + NADPH	diaphorase reaction	Spinacia oleracea	2 ferrocyanide + NADP+ + H+	-	?
2 ferricyanide + NADPH	diaphorase reaction	Anabaena sp.	2 ferrocyanide + NADP+ + H+	-	ir
additional information	the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible	Rhodobacter capsulatus	?	-	?
additional information	the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible	Anabaena sp.	?	-	?
additional information	the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible	Escherichia coli	?	-	?
additional information	the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible	Azotobacter vinelandii	?	-	?
NADPH + acceptor	the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Spinacia oleracea	NADP+ + reduced acceptor	-	?
NADPH + acceptor	the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Cyanobacteria	NADP+ + reduced acceptor	-	?
NADPH + acceptor	the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Zea mays	NADP+ + reduced acceptor	-	?
NADPH + acceptor	the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Capsicum annuum	NADP+ + reduced acceptor	-	?
NADPH + acceptor	the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide	Pisum sativum	NADP+ + reduced acceptor	-	?
reduced ferredoxin + NADP+	-	Escherichia coli	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	-	Rhodobacter capsulatus	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	-	Azotobacter vinelandii	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	-	Anabaena sp.	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction	Spinacia oleracea	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction	Pisum sativum	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction	Zea mays	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction	Capsicum annuum	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	enzyme catalyzes the final step of photosynthetic electron transfer fron the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation, enzyme is involved in dinitrogen fixation in heterocysts	Cyanobacteria	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	enzyme is involved in protection against oxidative stress, and in activation of anaerobic enzymes	Escherichia coli	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction, reaction is part of nitrogen assimilation in nonphotosynthetic tissues	Zea mays	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	release of oxidized ferredoxin is rate-limiting	Spinacia oleracea	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	release of oxidized ferredoxin is rate-limiting	Capsicum annuum	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	structure of the ferredoxin-enzyme complex, ferredoxin binds to the concave region of the FAD domain, overview, release of oxidized ferredoxin is rate-limiting	Zea mays	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting	Pisum sativum	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting	Zea mays	oxidized ferredoxin + NADPH	-	r
reduced ferredoxin + NADP+	structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting	Cyanobacteria	oxidized ferredoxin + NADPH	-	r

Subunits

Subunits	Comment	Organism
monomer	-	Escherichia coli
monomer	-	Spinacia oleracea
monomer	-	Pisum sativum
monomer	-	Zea mays
monomer	-	Rhodobacter capsulatus
monomer	-	Azotobacter vinelandii
monomer	-	Capsicum annuum
monomer	-	Anabaena sp.
monomer	-	Cyanobacteria

Synonyms

Synonyms	Comment	Organism
ferredoxin (flavodoxin)-NAD(P)H reductase	-	Escherichia coli
ferredoxin (flavodoxin)-NAD(P)H reductase	-	Spinacia oleracea
ferredoxin (flavodoxin)-NAD(P)H reductase	-	Pisum sativum
ferredoxin (flavodoxin)-NAD(P)H reductase	-	Zea mays
ferredoxin (flavodoxin)-NAD(P)H reductase	-	Rhodobacter capsulatus
ferredoxin (flavodoxin)-NAD(P)H reductase	-	Azotobacter vinelandii
ferredoxin (flavodoxin)-NAD(P)H reductase	-	Capsicum annuum
ferredoxin (flavodoxin)-NAD(P)H reductase	-	Anabaena sp.
ferredoxin (flavodoxin)-NAD(P)H reductase	-	Cyanobacteria
ferredoxin-NAD(P)H reductase	-	Escherichia coli
ferredoxin-NAD(P)H reductase	-	Spinacia oleracea
ferredoxin-NAD(P)H reductase	-	Pisum sativum
ferredoxin-NAD(P)H reductase	-	Zea mays
ferredoxin-NAD(P)H reductase	-	Rhodobacter capsulatus
ferredoxin-NAD(P)H reductase	-	Azotobacter vinelandii
ferredoxin-NAD(P)H reductase	-	Capsicum annuum
ferredoxin-NAD(P)H reductase	-	Anabaena sp.
ferredoxin-NAD(P)H reductase	-	Cyanobacteria
ferredoxin-NADP+ reductase	-	Escherichia coli
ferredoxin-NADP+ reductase	-	Spinacia oleracea
ferredoxin-NADP+ reductase	-	Pisum sativum
ferredoxin-NADP+ reductase	-	Zea mays
ferredoxin-NADP+ reductase	-	Rhodobacter capsulatus
ferredoxin-NADP+ reductase	-	Azotobacter vinelandii
ferredoxin-NADP+ reductase	-	Capsicum annuum
ferredoxin-NADP+ reductase	-	Anabaena sp.
ferredoxin-NADP+ reductase	-	Cyanobacteria
FNR	-	Escherichia coli
FNR	-	Spinacia oleracea
FNR	-	Pisum sativum
FNR	-	Zea mays
FNR	-	Rhodobacter capsulatus
FNR	-	Azotobacter vinelandii
FNR	-	Capsicum annuum
FNR	-	Anabaena sp.
FNR	-	Cyanobacteria
More	formerly termed thylakoid-bound diaphorase	Pisum sativum

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
41	-	inactivation of the reduced enzyme	Escherichia coli
66	-	inactivation of the oxidized enzyme	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
additional information	-	additional information	-	Escherichia coli
0.15	-	oxidized ferredoxin	with NADPH	Escherichia coli
27	-	NADPH	electron transfer via the enzyme to Fe(CN)63-	Escherichia coli
200	-	reduced ferredoxin	above, electron transfer via the enzyme to NADP+	Anabaena sp.
225	-	NADPH	electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c	Anabaena sp.
225	520	NADPH	electron transfer via the enzyme to K3Fe(CN)6	Anabaena sp.
250	-	NADPH	electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c	Spinacia oleracea
520	-	NADPH	electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c	Escherichia coli
550	-	NADPH	electron transfer via the enzyme to K3Fe(CN)6	Spinacia oleracea
600	-	reduced ferredoxin	electron transfer via the enzyme to NADP+	Spinacia oleracea

Cofactor

Cofactor	Comment	Organism
FAD	noncovalently bound prosthetic group	Escherichia coli
FAD	noncovalently bound prosthetic group	Spinacia oleracea
FAD	noncovalently bound prosthetic group	Pisum sativum
FAD	noncovalently bound prosthetic group	Zea mays
FAD	noncovalently bound prosthetic group	Rhodobacter capsulatus
FAD	noncovalently bound prosthetic group	Azotobacter vinelandii
FAD	noncovalently bound prosthetic group	Capsicum annuum
FAD	noncovalently bound prosthetic group	Anabaena sp.
FAD	noncovalently bound prosthetic group	Cyanobacteria
FAD	noncovalently bound prosthetic group, binding domain structure, ferredoxin binds to the concave region of the FAD domain	Zea mays
additional information	poor activity with NAD(H)	Escherichia coli
additional information	poor activity with NAD(H)	Spinacia oleracea
additional information	poor activity with NAD(H)	Pisum sativum
additional information	poor activity with NAD(H)	Zea mays
additional information	poor activity with NAD(H)	Rhodobacter capsulatus
additional information	poor activity with NAD(H)	Azotobacter vinelandii
additional information	poor activity with NAD(H)	Capsicum annuum
additional information	poor activity with NAD(H)	Anabaena sp.
additional information	poor activity with NAD(H)	Cyanobacteria
NADP+	binding domain structure of the plant-type enzyme, binding mechanism	Cyanobacteria
NADP+	binding domain structure, binding mechanism	Zea mays
NADP+	binding domain structure, binding mechanism	Capsicum annuum
NADP+	binding domain structure, binding mechanism, binding site structure and involved residues, overview	Spinacia oleracea
NADP+	binding domain structure, binding mechanism, binding site structure and involved residues, overview	Pisum sativum
NADP+	binding mechanism	Rhodobacter capsulatus
NADP+	binding mechanism	Azotobacter vinelandii
NADP+	binding mechanism	Anabaena sp.
NADP+	binding mechanism, cofactor is tightly bound, binding site structure and involved residues, overview	Escherichia coli
NADPH	binding domain structure of the plant-type enzyme, binding mechanism	Cyanobacteria
NADPH	binding domain structure, binding mechanism	Zea mays
NADPH	binding domain structure, binding mechanism	Capsicum annuum
NADPH	binding domain structure, binding mechanism, binding site structure and involved residues, overview	Spinacia oleracea
NADPH	binding domain structure, binding mechanism, binding site structure and involved residues, overview	Pisum sativum
NADPH	binding mechanism	Rhodobacter capsulatus
NADPH	binding mechanism	Azotobacter vinelandii
NADPH	binding mechanism	Anabaena sp.
NADPH	binding mechanism, cofactor is tightly bound, binding site structure and involved residues, overview	Escherichia coli