9E1J
Alpha-Delta heterodimeric form of soluble hydrogenase I from Pyrococcus furiosus. Data processed and model refined in P21221
Summary for 9E1J
| Entry DOI | 10.2210/pdb9e1j/pdb |
| Descriptor | Sulfhydrogenase 1 subunit delta, Sulfhydrogenase 1 subunit alpha, IRON/SULFUR CLUSTER, ... (7 entities in total) |
| Functional Keywords | ni-fe hydrogenase, lyase |
| Biological source | Pyrococcus furiosus More |
| Total number of polymer chains | 4 |
| Total formula weight | 154927.48 |
| Authors | |
| Primary citation | Xiao, X.,Schut, G.J.,Feng, X.,McTernan, P.M.,Haja, D.K.,Lanzilotta, W.N.,Adams, M.W.W.,Li, H. Structural insights into the biotechnologically relevant reversible NADPH-oxidizing NiFe-hydrogenase from P.furiosus. Structure, 2025 Cited by PubMed Abstract: 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. PubMed: 40570843DOI: 10.1016/j.str.2025.05.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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