1.19.1.1	2 ferricyanide + NADPH	-	Escherichia coli	2 ferrocyanide + NADP+ + H+	-	?	230338	
1.19.1.1	2 ferricyanide + NADPH	-	Rhodobacter capsulatus	2 ferrocyanide + NADP+ + H+	-	?	230338	
1.19.1.1	2 ferricyanide + NADPH	-	Escherichia coli HMS174	2 ferrocyanide + NADP+ + H+	-	?	230338	
1.19.1.1	2 ferricyanide + NADPH + H+	-	Rhodobacter capsulatus	2 ferrocyanide + NADP+ + H+	-	?	436723	
1.19.1.1	2 ferricyanide + NADPH + H+	-	Rhodobacter capsulatus 37b4	2 ferrocyanide + NADP+ + H+	-	?	436723	
1.19.1.1	2 ferricytochrome c + NADPH + H+	-	Rhodobacter capsulatus	2 ferrocytochrome c + NADP+ + H+	-	?	436724	
1.19.1.1	2 ferricytochrome c2 + NADPH	-	Escherichia coli	2 ferrocytochrome c2 + NADP+ + H+	-	?	287652	
1.19.1.1	2 ferricytochrome c2 + NADPH	-	Escherichia coli HMS174	2 ferrocytochrome c2 + NADP+ + H+	-	?	287652	
1.19.1.1	2,6-dichlorophenolindophenol + NADPH	-	Rhodobacter capsulatus	reduced 2,6-dichlorophenolindophenol + NADP+	-	?	436744	
1.19.1.1	FMNH2 + NADP+	-	Escherichia coli	FMN + NADPH + H+	-	?	415643	
1.19.1.1	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	Escherichia coli	?	-	?	89	
1.19.1.1	additional information	enzyme additionally shows diaphorase activity which is induced by treatment with methyl viologen	Rhodobacter capsulatus	?	-	?	89	
1.19.1.1	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	Nostoc sp.	?	-	?	89	
1.19.1.1	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	Escherichia coli	?	-	?	89	
1.19.1.1	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	Escherichia coli	?	-	?	89	
1.19.1.1	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	Escherichia coli B / ATCC 11303	?	-	?	89	
1.19.1.1	additional information	enzyme additionally shows diaphorase activity which is induced by treatment with methyl viologen	Rhodobacter capsulatus 37b4	?	-	?	89	
1.19.1.1	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	Nostoc sp. ATCC 29151	?	-	?	89	
1.19.1.1	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	Escherichia coli HMS174	?	-	?	89	
1.19.1.1	oxidized cytochrome c + NADH + H+	-	Escherichia coli	reduced cytochrome c + NAD+	-	r	437787	
1.19.1.1	oxidized cytochrome c + NADH + H+	-	Escherichia coli HMS174	reduced cytochrome c + NAD+	-	r	437787	
1.19.1.1	oxidized cytochrome c + NADPH + H+	-	Escherichia coli	reduced cytochrome c + NADP+	-	r	437788	
1.19.1.1	oxidized cytochrome c + NADPH + H+	-	Escherichia coli HMS174	reduced cytochrome c + NADP+	-	r	437788	
1.19.1.1	reduced 2,6-dichlorophenolindophenol + NADP+	-	Escherichia coli	oxidized 2,6-dichlorophenolindophenol + NADPH + H+	-	?	437866	
1.19.1.1	reduced flavodoxin + NADP+	-	Escherichia coli	oxidized flavodoxin + NADPH + H+	-	?	437867	
1.19.1.1	reduced flavodoxin + NADP+	-	Pisum sativum	oxidized flavodoxin + NADPH + H+	-	?	437867	
1.19.1.1	reduced flavodoxin + NADP+	-	Nostoc sp.	oxidized flavodoxin + NADPH + H+	-	?	437867	
1.19.1.1	reduced flavodoxin + NADP+	-	Nostoc sp. ATCC 29151	oxidized flavodoxin + NADPH + H+	-	?	437867	
1.19.1.1	reduced flavodoxin + NADP+	-	Escherichia coli HMS174	oxidized flavodoxin + NADPH + H+	-	?	437867	
1.19.1.1	reduced flavodoxin I + NADP+	-	Escherichia coli	oxidized flavodoxin I + NADPH + H+	-	?	436561	
1.19.1.1	reduced flavodoxin II + NADP+	-	Escherichia coli	oxidized flavodoxin II + NADPH + H+	-	?	436562