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Literature summary extracted from

  • Senda, M.; Kishigami, S.; Kimura, S.; Senda, T.
    Crystallization and preliminary X-ray analysis of the electron-transfer complex of Rieske-type [2Fe-2S] ferredoxin and NADH-dependent ferredoxin reductase derived from Acidovorax sp. strain KKS102 (2007), Acta Crystallogr. Sect. F, 63, 520-523.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.1.3 overexpression of BphA4 in Escherichia coli JM109 cells Acidovorax sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.18.1.3 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 Acidovorax sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.3 ferredoxin + NADH Acidovorax sp. BphA3, a Rieske-type [2Fe-2S] ferredoxin, and BphA4 comprise an electron-transfer system for the multi-component dioxygenase BphA, BphA4 receives two electrons from NADH as a form of hydride and transfers an electron to each of two BphA3 molecules, molecular mechanism of the electron transfer between BphA3 and BphA4, overview reduced ferredoxin + NAD+ + H+
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 ?

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.3 Acidovorax sp.
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 Pseudomonas sp., strain KKS102
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Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.1.3 recombinant BphA4 under aerobic conditions from Escherichia coli JM109 cells by anion exchange and adsorption chromatography, and ultrafiltration Acidovorax sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.3 ferredoxin + NADH BphA3, a Rieske-type [2Fe-2S] ferredoxin, and BphA4 comprise an electron-transfer system for the multi-component dioxygenase BphA, BphA4 receives two electrons from NADH as a form of hydride and transfers an electron to each of two BphA3 molecules, molecular mechanism of the electron transfer between BphA3 and BphA4, overview Acidovorax sp. reduced ferredoxin + NAD+ + H+
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 ?
1.18.1.3 additional information the enzyme BphA4 is an FAD-containing NADHdependent ferredoxin reductase Acidovorax sp. ?
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 ?

Subunits

EC Number Subunits Comment Organism
1.18.1.3 More BphA3, a Rieske-type [2Fe-2S] ferredoxin, and BphA4 comprise an electron-transfer system for the multi-component dioxygenase BphA Acidovorax sp.

Synonyms

EC Number Synonyms Comment Organism
1.18.1.3 BphA4
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 Acidovorax sp.
1.18.1.3 NADH-dependent ferredoxin reductase
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 Acidovorax sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.3 NADPH
-
 Acidovorax sp.