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

Research output: Contribution to journalArticle

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Abstract

[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.

Original languageEnglish
Pages (from-to)29-40
Number of pages12
JournalMolecular Cell
Volume27
Issue number1
DOIs
Publication statusPublished - Jul 6 2007

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Sulfhydryl Compounds
Oxidation-Reduction
Catalytic Domain
Iron
Thermococcus
Cysteine
Proteins
Adenosine Triphosphate
Binding Sites
ferredoxin-thioredoxin reductase
nickel-iron hydrogenase

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Cite this

Crystal Structures of [NiFe] Hydrogenase Maturation Proteins HypC, HypD, and HypE : Insights into Cyanation Reaction by Thiol Redox Signaling. / Watanabe, Satoshi; Matsumi, Rie; Arai, Takayuki; Atomi, Haruyuki; Imanaka, Tadayuki; Miki, Kunio.

In: Molecular Cell, Vol. 27, No. 1, 06.07.2007, p. 29-40.

Research output: Contribution to journalArticle

Watanabe, Satoshi ; Matsumi, Rie ; Arai, Takayuki ; Atomi, Haruyuki ; Imanaka, Tadayuki ; Miki, Kunio. / Crystal Structures of [NiFe] Hydrogenase Maturation Proteins HypC, HypD, and HypE : Insights into Cyanation Reaction by Thiol Redox Signaling. In: Molecular Cell. 2007 ; Vol. 27, No. 1. pp. 29-40.
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abstract = "[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 {\AA}, 2.07 {\AA}, and 1.55 {\AA} 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.",
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