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1.3.7.7: ferredoxin:protochlorophyllide reductase (ATP-dependent)

This is an abbreviated version!
For detailed information about ferredoxin:protochlorophyllide reductase (ATP-dependent), go to the full flat file.

Word Map on EC 1.3.7.7

Reaction

chlorophyllide a
+
oxidized ferredoxin
+
2 ADP
+ 2 phosphate =
protochlorophyllide a
+
reduced ferredoxin
+ 2 ATP + 2 H2O

Synonyms

bchB, bchL, bchN, ChlB, ChlL, ChlN, dark operative protochlorophyllide oxidoreductase, dark protochlorophyllide reductase, dark-operative DPOR, dark-operative Pchlide oxidoreductase, dark-operative protochlorophyllide oxidoreductase, dark-operative protochlorophyllide reductase, DPOR, light-independent (dark) Pchlide reductase, light-independent (dark-operative) Pchlide oxidoreductase, light-independent Pchlide oxidoreductase, light-independent Pchlide reductase, light-independent protochlorophyllide oxidoreductase, light-independent protochlorophyllide oxidoreductases, light-independent protochlorophyllide reductase, LIPOR, PORA, protochlorophyllide oxidoreductase, protochlorophyllide oxidoreductase complex

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.7 With an iron-sulfur protein as acceptor
                1.3.7.7 ferredoxin:protochlorophyllide reductase (ATP-dependent)

Crystallization

Crystallization on EC 1.3.7.7 - ferredoxin:protochlorophyllide reductase (ATP-dependent)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
L-protein in the MgADP-bound form, X-ray diffraction structure determination at 1.6 A resolution
-
L-protein of DPOR with Mg-ADP bound, microcapillary batch diffusion method, with 20-25% (w/v) PEG 3350 as the precipitating agent, with 200 mM magnesium formate (pH 7.7)
substrate-bound, ADP-aluminium fluoride-stabilized transition state complex between the DPOR components L2 and (NB)2, sitting drops by vapor diffusion, mixing of 0.001 ml of protein solution containing 7.5 mg/ml protein in 100 mM HEPES/NaOH, pH 7.5, 150 mM NaCl, 10 mM MgCl2, 50 mM NaF, and 2 mM AlCl3,with 0.001 ml of reservoir solution containing 0.1 M KCl, 0.1 M Tris, pH 8.5, and 3% wt/v PEG 6000, 17°C, X-ray diffraction structure determination and analysis at 2.1 A resolution
catalytic component NB-protein, both in thePchlide-bound and Pchlide-free states, X-ray diffraction structure determination at 2.3 A and 2.8 A resolution, respectively
-
hanging drop vapor diffusion method, the protochlorophyllide-bound form of NB-protein is crystallized using 200 mM sodium/potassium phosphate buffer (pH 5.0) containing 5 mM dithiothreitol and 10% (w/v) ethylene glycol at 4°C, to which 16% (w/v) and 14% (w/v) PEG4K are added in aerobic and anaerobic conditions, respectively, as precipitants. Protochlorophyllide -free and selenomethionine-substituted recombinant NB-proteins are crystallized at 20°C using 20% (w/v) PEG3350 containing 200 mM ammonium chloride and 5mM dithiothreitol. D36C and D36A variants are crystallized at 4°C using 20% (w/v) PEG3350 containing 200 mM sodium chloride, 100 mM MOPS/NaOH (pH 7.0) and 5 mM dithiothreitol as a precipitant
-
purified recombinant protochlorophyllide-bound and protochlorophyllide-free forms of NB-protein of DPOR, and purified recombinant selenomethionine-substituted protochlorophyllide-free forms of mutants D36A and D36C, hanging-drop vapour diffusion method., X-ray diffraction structure determination and analysis at 2.3-2.9 A resolution
-
native and SeMet-labeled catalytic (ChlN/ChlB)2 complex, hanging drop vapor diffusion, 17°C, mixing of 0.003 ml of 10 mg/ml protein in 100 mM HEPES-NaOH, pH 7.5, 150 mM NaCl, and 10 mM MgCl2, with 0.003 ml of reservoir solution consisting of 9.5% PEG 6000, 85 mM HEPES-NaOH, pH 7.1, 14.3% 2-methyl pentane-2,4-diol, and 15% glycerol as cryoprotectants or 10.5% PEG 6000, 85 mM HEPES-NaOH, pH7.5, 14.3% 2-methyl pentane-2,4-diol, and 15% glycerol as cryoprotectants for selenomethionine-labeled protein, 3-5 days,X-ray diffraction structure determination and analysis at 2.4-2.81 A resolution
Thermosynechococcus vestitus
-