The flavin reductase ActVB from Streptomyces coelicolor: characterization of the electron transferase activity of the flavoprotein form.
The flavin reductase ActVB is involved in the last step of actinorhodin biosynthesis in Streptomyces coelicolor. Although ActVB can be isolated with some FMN bound, this form was not involved in the flavin reductase activity. By studying the ferric reductase activity of ActVB, we show that its FMN-bound form exhibits a proper enzymatic activity of reduction of iron complexes by NADH. This shows that ActVB active site exhibits a dual property with regard to the FMN. It can use it as a substrate that goes in and off the active site or as a cofactor to provide an electron transferase activity to the polypeptide.
Filisetti
Laurent
L
Laboratoire de Chimie et Biochimie des Centres Redox Biologiques, DRDC-CEA/CNRS/Université Joseph Fourier, Grenoble, France.
Valton
Julien
J
Fontecave
Marc
M
Nivière
Vincent
V
D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D010088:Oxidoreductases / Q000378:metabolism*; D048372:Streptomyces coelicolor / Q000201:enzymology*
D001426:Bacterial Proteins; D010088:Oxidoreductases