29EI
[FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant E278Q
Summary for 29EI
| Entry DOI | 10.2210/pdb29ei/pdb |
| Descriptor | Iron hydrogenase 1, dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+), IRON/SULFUR CLUSTER, ... (8 entities in total) |
| Functional Keywords | [fefe]-hydrogenase cpi from clostridium pasteurianum, variant e278q, oxidoreductase |
| Biological source | Clostridium pasteurianum |
| Total number of polymer chains | 2 |
| Total formula weight | 134589.64 |
| Authors | Duan, J.,Yang, Z.,Zheng, F.,Hofmann, E.,Happe, T. (deposition date: 2026-03-09, release date: 2026-10-28) |
| Primary citation | Duan, J.,Yang, Z.,Lampret, O.,Arrigoni, F.,Impel, L.V.,Zheng, F.,Kleinhaus, J.,Apfel, U.P.,Greco, C.,De Gioia, L.,Hofmann, E.,Hemschemeier, A.,Happe, T. A Histidine-Mediated, Pendulum-Like Proton Transport Mechanism Is Required for the High Catalytic Activity of [FeFe]-Hydrogenases J.Am.Chem.Soc., 2026 Cited by DOI: 10.1021/jacs.6c14410PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.31 Å) |
Structure validation
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