HydF as a scaffold protein in [FeFe] hydrogenase H-cluster biosynthesis

详细信息    查看全文

• 作者：Shawn E. McGlynn ; Eric M. Shepard ; Mark A. Winslow ; Anatoli V. Naumov ; Kaitlin S. Duschene ; Matthew C. Posewitz ; William E. Broderick ; Joan B. Broderick ; John W. Peters
• 关键词：Hydrogenase ; Metalloenzyme ; Iron– ; sulfur cluster maturation ; H-cluster ; Scaffold
• 刊名：FEBS Letters
• 出版年：2008
• 出版时间：25 June 2008
• 年：2008
• 卷：582
• 期：15
• 页码：2183-2187
• 全文大小：246 K

文摘

In an effort to determine the specific protein component(s) responsible for in vitro activation of the [FeFe] hydrogenase (HydA), the individual maturation proteins HydE, HydF, and HydG from Clostridium acetobutylicum were purified from heterologous expressions in Escherichia coli. Our results demonstrate that HydF isolated from a strain expressing all three maturation proteins is sufficient to confer hydrogenase activity to purified inactive heterologously expressed HydA (expressed in the absence of HydE, HydF, and HydG). These results represent the first in vitro maturation of [FeFe] hydrogenase with purified proteins, and suggest that HydF functions as a scaffold upon which an H-cluster intermediate is synthesized.