Cloned (Comment) | Organism |
---|---|
overexpression of BphA4 in Escherichia coli JM109 cells | Acidovorax sp. |
Crystallization (Comment) | Organism |
---|---|
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acidovorax sp. | - |
Pseudomonas sp., strain KKS102 | - |
Purification (Comment) | Organism |
---|---|
recombinant BphA4 under aerobic conditions from Escherichia coli JM109 cells by anion exchange and adsorption chromatography, and ultrafiltration | Acidovorax sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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+ | - |
? | |
additional information | the enzyme BphA4 is an FAD-containing NADHdependent ferredoxin reductase | Acidovorax sp. | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | BphA3, a Rieske-type [2Fe-2S] ferredoxin, and BphA4 comprise an electron-transfer system for the multi-component dioxygenase BphA | Acidovorax sp. |
Synonyms | Comment | Organism |
---|---|---|
BphA4 | - |
Acidovorax sp. |
NADH-dependent ferredoxin reductase | - |
Acidovorax sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Acidovorax sp. |