Crystal Structures of [NiFe] Hydrogenase Maturation Proteins HypC, HypD, and HypE: Insights into Cyanation Reaction by Thiol Redox Signaling

Satoshi Watanabe, Rie Matsumi, Takayuki Arai, Haruyuki Atomi, Tadayuki Imanaka, Kunio Miki

研究成果: Article査読

79 被引用数 (Scopus)

抄録

[NiFe] hydrogenase maturation proteins HypC, HypD, and HypE catalyze the insertion and cyanation of the iron center of [NiFe] hydrogenases by an unknown mechanism. We have determined the crystal structures of HypC, HypD, and HypE from Thermococcus kodakaraensis KOD1 at 1.8 Å, 2.07 Å, and 1.55 Å resolution, respectively. The structure of HypD reveals its probable iron binding and active sites for cyanation. An extended conformation of each conserved motif of HypC and HypE allows the essential cysteine residues of both proteins to interact with the active site of HypD. Furthermore, the C-terminal tail of HypE is shown to exist in an ATP-dependent dynamic equilibrium between outward and inward conformations. Unexpectedly, the [4Fe-4S] cluster environment of HypD is quite similar to that of ferredoxin:thioredoxin reductase (FTR), indicating the existence of a redox cascade similar to the FTR system. These results suggest a cyanation reaction mechanism via unique thiol redox signaling in the HypCDE complex.

本文言語English
ページ(範囲)29-40
ページ数12
ジャーナルMolecular Cell
27
1
DOI
出版ステータスPublished - 2007 7 6
外部発表はい

ASJC Scopus subject areas

  • 分子生物学
  • 細胞生物学

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