7QHF
[FeFe]-hydrogenase I from Clostridium pasteurianum (CpI), variant G302S
Summary for 7QHF
| Entry DOI | 10.2210/pdb7qhf/pdb |
| Related | 7QHC |
| Descriptor | Iron hydrogenase 1, dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+), IRON/SULFUR CLUSTER, ... (7 entities in total) |
| Functional Keywords | [fefe]-hydrogenase i from clostridium pasteurianum (cpi), variant g302s, oxidoreductase |
| Biological source | Clostridium pasteurianum |
| Total number of polymer chains | 2 |
| Total formula weight | 134438.94 |
| Authors | Brocks, C.,Duan, J.,Hofmann, E.,Happe, T. (deposition date: 2021-12-12, release date: 2023-09-27, Last modification date: 2023-11-29) |
| Primary citation | Brocks, C.,Das, C.K.,Duan, J.,Yadav, S.,Apfel, U.P.,Ghosh, S.,Hofmann, E.,Winkler, M.,Engelbrecht, V.,Schafer, L.V.,Happe, T. A Dynamic Water Channel Affects O 2 Stability in [FeFe]-Hydrogenases. Chemsuschem, :e202301365-e202301365, 2023 Cited by PubMed Abstract: [FeFe]-hydrogenases are capable of reducing protons at a high rate. However, molecular oxygen (O ) induces the degradation of their catalytic cofactor, the H-cluster, which consists of a cubane [4Fe4S] subcluster (4Fe ) and a unique diiron moiety (2Fe ). Previous attempts to prevent O -induced damage have focused on enhancing the protein's sieving effect for O by blocking the hydrophobic gas channels that connect the protein surface and the 2Fe . In this study, we aimed to block an O diffusion pathway and shield 4Fe instead. Molecular dynamics (MD) simulations identified a novel water channel (W ) surrounding the H-cluster. As this hydrophilic path may be accessible for O molecules we applied site-directed mutagenesis targeting amino acids along W in proximity to 4Fe to block O diffusion. Protein film electrochemistry experiments demonstrate increased O stabilities for variants G302S and S357T, and MD simulations based on high-resolution crystal structures confirmed an enhanced local sieving effect for O in the environment of the 4Fe in both cases. The results strongly suggest that, in wild type proteins, O diffuses from the 4Fe to the 2Fe . These results reveal new strategies for improving the O stability of [FeFe]-hydrogenases by focusing on the O diffusion network near the active site. PubMed: 37830175DOI: 10.1002/cssc.202301365 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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