1.18.1.3: ferredoxin-NAD+ reductase
This is an abbreviated version!
For detailed information about ferredoxin-NAD+ reductase, go to the full flat file.
Word Map on EC 1.18.1.3
Reaction
+
+
=
+
Synonyms
BphA4, FdR, Fdx-FdR, ferredoxin NADPH reductase, ferredoxin-linked NAD reductase, ferredoxin-NAD reductase, ferredoxin-NAD(P)H reductase, ferredoxin-NAD+ reductase, ferredoxin-NADH oxidoreductase, ferredoxin-reductase, ferredoxin/flavodoxin-NAD+ reductase, More, NAD-ferredocinTOL reductase, NAD-ferredoxin reductase, NADH flavodoxin oxidoreductase, NADH-dependent ferredoxin reductase, NADH-ferredoxin oxidoreductase, NADH-ferredoxin reductase, NADH-ferredoxinNAP reductase, NADH2-ferredoxin oxidoreductase, palustrisredoxin reductase, PuR, Red, RedIIA, reductase, ferredoxin, reductase, ferredoxin-nicotinamide adenine dinucleotide, reductase, reduced nicotinamide adenine dinucleotide-ferredoxin, Rnf, XYLA, xylM
ECTree
Cofactor
Cofactor on EC 1.18.1.3 - ferredoxin-NAD+ reductase
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additional information
no activity with NADPH
-
FAD
-
-
FAD
-
can bind one mol of FAD per mol of enzyme, Km: 2.5 nM
FAD
-
1 mol of FAD is bound per mol of enzyme
FAD
-
contains 0.89 mol of FAD per mol of enzyme
FAD
-
associated to enzyme, 0.6-0.8 FAD per protein monomer
FAD
-
spectral maxima at 273, 378 and 452 nm, 0.75 mol of FAD per mol of protein
FAD
1 mol/mol enzyme. The electron flow is from NADH to FAD to [2Fe-2S]
FAD
1.07 mol/mol of enzyme
Ferredoxin
-
-
-
Ferredoxin
enzyme reduces ferredoxin with the concomitant oxidation of NADH
-
NAD+
-
-
NAD+
Oleidesulfovibrio alaskensis
-
-
NADH
-
-
NADH
-
preferred cofactor
NADH
-
the CO-adapted strain is a metabolic mutant having higher levels of ferredoxin-NAD+ oxidoreductase activity, which is not inhibited by NADH
NADH
electron-transfer component XylA. The electron flow is from NADH to FAD to [2Fe-2S]
NADH
enzyme reduces ferredoxin with the concomitant oxidation of NADH
NADPH
-
-
NADPH
-
39% of the activity with NADH in the reaction with cytochrome c
NADPH
-
much less effective cofactor than NADH
[2Fe-2S]-center
presence of one [2Fe-2S] center per enzyme molecule
[2Fe-2S]-center
protein contains 2 mol/mol of non-haem iron and 2 mol/mol of acid-labile sulfide. The electron flow is from NADH to FAD to [2Fe-2S]