Literature summary for 1.18.1.3 extracted from

Peng, Y.; Xu, F.; Bell, S.G.; Wong, L.L.; Rao, Z.
Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009 (2007), Acta Crystallogr. Sect. F, 63, 422-425.

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of PuR in Escherichia coli strain BL21(DE3) using the tandem tac promoters in the pCWori+ vector	Rhodopseudomonas palustris

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Rhodopseudomonas palustris

Crystallization (Comment)

Organism

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

Rhodopseudomonas palustris

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	in an iron-sulfur center	Rhodopseudomonas palustris

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ferredoxin + NADH	Rhodopseudomonas palustris	the enzyme is an essential component of the cytochrome P450 systems in Rhodopseudomonas palustris strain CGA009, a model organism with diverse metabolic pathways	reduced ferredoxin + NAD+ + H+	-	?
ferredoxin + NADH	Rhodopseudomonas palustris CGA009	the enzyme is an essential component of the cytochrome P450 systems in Rhodopseudomonas palustris strain CGA009, a model organism with diverse metabolic pathways	reduced ferredoxin + NAD+ + H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Rhodopseudomonas palustris	-	-	-
Rhodopseudomonas palustris CGA009	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia col strain BL21(DE3) by repeated anion exchange chromatography, using a linear gradient of NaCl in 20 mM HEPES buffer, pH 7.0, for elution, followed by gel filtration and ultrafiltration	Rhodopseudomonas palustris

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ferredoxin + NADH	the enzyme is an essential component of the cytochrome P450 systems in Rhodopseudomonas palustris strain CGA009, a model organism with diverse metabolic pathways	Rhodopseudomonas palustris	reduced ferredoxin + NAD+ + H+	-	?
ferredoxin + NADH	electron transport is initiated by a single two-electron transfer from NAD(P)H to FAD to produce fully reduced FADH2, which provides one electron to the iron-sulfur cluster, in most cases a [2Fe2S] cluster, of ferredoxins. These electrons are finally transferred to the terminal oxygenase, mechanism of electron transport, overview	Rhodopseudomonas palustris	reduced ferredoxin + NAD+ + H+	-	?
ferredoxin + NADH	the enzyme is an essential component of the cytochrome P450 systems in Rhodopseudomonas palustris strain CGA009, a model organism with diverse metabolic pathways	Rhodopseudomonas palustris CGA009	reduced ferredoxin + NAD+ + H+	-	?
ferredoxin + NADH	electron transport is initiated by a single two-electron transfer from NAD(P)H to FAD to produce fully reduced FADH2, which provides one electron to the iron-sulfur cluster, in most cases a [2Fe2S] cluster, of ferredoxins. These electrons are finally transferred to the terminal oxygenase, mechanism of electron transport, overview	Rhodopseudomonas palustris CGA009	reduced ferredoxin + NAD+ + H+	-	?

Subunits

Subunits	Comment	Organism
monomer	dynamic light scattering of PuR	Rhodopseudomonas palustris

Synonyms

Synonyms	Comment	Organism
BphA4	-	Rhodopseudomonas palustris
ferredoxin-NAD(P)H reductase	-	Rhodopseudomonas palustris
ferredoxin-reductase	-	Rhodopseudomonas palustris
More	the enzyme is a member of the oxygenase-coupled NADH-dependent ferredoxin reductase family of FAD-dependent electron-transfer enzymes	Rhodopseudomonas palustris
palustrisredoxin reductase	-	Rhodopseudomonas palustris
PuR	-	Rhodopseudomonas palustris

Cofactor

Cofactor	Comment	Organism	Structure
FAD	dependent on	Rhodopseudomonas palustris
NADH	-	Rhodopseudomonas palustris