The flavin reductase ActVB from Streptomyces coelicolor:: Characterization of the electron transferase activity of the flavoprotein form

被引:14
作者
Filisetti, L [1 ]
Valton, J [1 ]
Fontecave, M [1 ]
Nivière, V [1 ]
机构
[1] Univ Grenoble 1, CNRS, CEA,Ctr Redox Biol, DRDC,Lab Chim & Biochim, F-38054 Grenoble, France
来源
FEBS LETTERS | 2005年 / 579卷 / 13期
关键词
ActVB from Streptomyces coelicolor; flavin reductase; FMN substrate; FMN cofactor; ferric reductase; two-substrates enzyme mechanism;
D O I
10.1016/j.febslet.2005.04.019
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2817 / 2820
页数:4
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