Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

reduced ferredoxin
+
NAD+
+
H+
=
oxidized ferredoxin
+
NADH

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

     1 Oxidoreductases
         1.18 Acting on iron-sulfur proteins as donors
             1.18.1 With NAD+ or NADP+ as acceptor
                1.18.1.3 ferredoxin-NAD+ reductase

Crystallization

Crystallization on EC 1.18.1.3 - ferredoxin-NAD+ reductase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant BphA4 in complex with BphA3, anaerobic crystallization is essential to crystallize the productive complex between oxidized BphA3 and NADH-reduced BphA4, sitting-drop vapour-diffusion method, 26.4 mg/ml BphA4 in 50 mM potassium phosphate buffer, pH 7.0, is reduced with 20 mM NADH for 5 min at 4°C, and mixed with oxidized BphA3 at a concentration of 17.5 mg/ml, mixing of 0.9 ml of each of the protein and reservoir solutions, and equilibration against 500 ml reservoir solution, containing 0.2 M ammonium acetate, 0.1 M sodium citrate, pH 5.6, 30% w/v PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
recombinant His-tagged RedIIA from KA1, hanging-drop vapour-diffusion, 5°C, method using PEG 4000, X-ray diffraction structure determination and analysis at 1.58 A resolution, modelling
-
ferredoxin reductase component of biphenyl dioxygenase
-
purified recombinant enzyme, hanging-drop vapour-diffusion method, 0.001 ml of protein solution with 20mg/ml protein in 20 mM HEPES, pH 7.0, and 0.001 ml reservoir solution, containing 100 mM HEPES, pH 7.0-7.2, 16-18% w/v PEG 10 000 at 18°C, are mixed and equilibrated against 200 ml reservoir solution, 70 mM sodium cacodylate pH 6.5, 0.98 M sodium acetate, 30% v/v glycerol are best for cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement using the putidaredoxin reductase structure, overview
-