EC Number   |
Subunits |
Reference |
|---|
   1.18.1.5 | dimer |
both WT and His6-Pdr undergo a monomer-dimer association-dissociation |
717764 |
| 1.18.1.5 | dimer |
x-ray crystallography |
681373 |
| 1.18.1.5 | monomer |
both WT and His6-Pdr undergo a monomer-dimer association-dissociation |
717764 |
| 1.18.1.5 | More |
cross-linking of putidaredoxin and putidaredoxin reductase by 1-ethyl 3-[3-(dimethylamino)propyl]carbodiimide, EDC. EDC promotes formation of stoichiometric Pdr-Pdx complexes only when carboxyl groups on putidaredoxin are activated. The putidaredoxin-putidaredoxin reductase C73S/C85S conjugate protein is more efficient in electron transfer to cytochrome c and, in the presence of saturating levels of P450cam, more effectively supports camphor hydroxylation. The cross-linked complex is physiologically relevant and represents a suitable model for mechanistic studies, and molecular recognition between putidaredoxin and putidaredoxin reductase is redox-controlled and assisted by the putidaredoxin Glu72 and putidaredoxin reducase Lys409 charge-charge interactions |
717251 |
| 1.18.1.5 | More |
Pdr-Pdx complex formation is mainly driven by steric complementarity, bulky side chains of Tyr33, Arg66, and Trp106 prevent tight binding of oxidized Pdx and facilitate dissociation of the reduced iron-sulfur protein from Pdr |
717770 |
