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TitleStructural insights into the biotechnologically relevant reversible NADPH-oxidizing NiFe-hydrogenase from P.furiosus.
Journal, issue, pagesStructure, Year 2025
Publish dateJun 20, 2025
AuthorsXiansha Xiao / Gerrit J Schut / Xiang Feng / Patrick M McTernan / Dominik K Haja / William N Lanzilotta / Michael W W Adams / Huilin Li /
PubMed AbstractThe cytoplasmic hydrogenase I (SHI) from the hyperthermophilic archaeon Pyrococcus furiosus belongs to the group III hydrogenase family. SHI oxidizes NADPH rather than NADH to reduce protons and ...The cytoplasmic hydrogenase I (SHI) from the hyperthermophilic archaeon Pyrococcus furiosus belongs to the group III hydrogenase family. SHI oxidizes NADPH rather than NADH to reduce protons and evolve hydrogen gas, and because of this property, coupled with its high thermal stability, the enzyme holds great potential for economical hydrogen production. Despite decades of efforts, the SHI structure has remained unknown. Here, we report the cryoelectron microscopic (cryo-EM) structures of the heterotetrameric SHI holoenzyme (αδβγ). SHI is a symmetric dimer of two individually functional heterotetramers. SHI-αδ resembles the standard [NiFe] hydrogenase, and SHI-βγ function as the NADPH oxidoreductase. SHI-β contains three [4Fe-4S] clusters that relay electrons from NADPH in SHI-γ to the catalytic [NiFe] cluster in SHI-αδ for H production. These structures will guide the adaptation of this unique enzyme for biotechnological applications.
External linksStructure / PubMed:40570843
MethodsEM (single particle)
Resolution3.06 - 3.53 Å
Structure data

49340

9nez

EMDB-49340: Cryo-EM map of the Pyrococcus furiosus SHI complex
PDB-9nez: Structure of the Pyrococcus furiosus SHI complex
Method: EM (single particle) / Resolution: 3.47 Å

49341

9nf0

EMDB-49341: Cryo-EM composite map of the NADPH-bound Pyrococcus furiosus SHI complex
PDB-9nf0: Structure of the NADPH-bound Pyrococcus furiosus SHI complex
Method: EM (single particle) / Resolution: 3.06 Å

EMDB-49342: Cryo-EM consensus map of the NADPH-bound Pyrococcus furiosus SHI complex
Method: EM (single particle) / Resolution: 3.06 Å

EMDB-49343: Cryo-EM focus map of the NADPH-bound Pyrococcus furiosus SHI complex
Method: EM (single particle) / Resolution: 3.53 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-NFU:
formyl[bis(hydrocyanato-1kappaC)]ironnickel(Fe-Ni)

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-MG:
Unknown entry

Source
  • pyrococcus furiosus (archaea)
KeywordsELECTRON TRANSPORT / hydrogen production / [NiFe] hydrogenase / cryo-EM structure

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