6G94
Structure of E. coli hydrogenase-1 C19G variant in complex with cytochrome b
Summary for 6G94
Entry DOI | 10.2210/pdb6g94/pdb |
Related | 3UQY 3USC 3USE 4GD3 |
Descriptor | Hydrogenase-1 small chain, CHLORIDE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (12 entities in total) |
Functional Keywords | new [4fe-4s] cluster, oxidoreductase |
Biological source | Escherichia coli K-12 More |
Total number of polymer chains | 10 |
Total formula weight | 467579.08 |
Authors | Volbeda, A.,Fontecilla-Camps, J.C. (deposition date: 2018-04-10, release date: 2018-06-13, Last modification date: 2024-01-17) |
Primary citation | Volbeda, A.,Mouesca, J.M.,Darnault, C.,Roessler, M.M.,Parkin, A.,Armstrong, F.A.,Fontecilla-Camps, J.C. X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe-4S] cluster. Chem. Commun. (Camb.), 54:7175-7178, 2018 Cited by PubMed Abstract: The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni-Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype. PubMed: 29888350DOI: 10.1039/c8cc02896f PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report