5LA3
[FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant E279A
Summary for 5LA3
| Entry DOI | 10.2210/pdb5la3/pdb |
| Descriptor | Iron hydrogenase 1, dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+), IRON/SULFUR CLUSTER, ... (6 entities in total) |
| Functional Keywords | hydrogenase, h-cluster, oxidoreductase, semisynthetic enzyme |
| Biological source | Clostridium pasteurianum |
| Total number of polymer chains | 2 |
| Total formula weight | 133767.63 |
| Authors | Duan, J.,Esselborn, J.,Hofmann, E.,Winkler, M.,Happe, T. (deposition date: 2016-06-13, release date: 2017-06-21, Last modification date: 2024-01-10) |
| Primary citation | Winkler, M.,Senger, M.,Duan, J.,Esselborn, J.,Wittkamp, F.,Hofmann, E.,Apfel, U.P.,Stripp, S.T.,Happe, T. Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases. Nat Commun, 8:16115-16115, 2017 Cited by PubMed Abstract: H turnover at the [FeFe]-hydrogenase cofactor (H-cluster) is assumed to follow a reversible heterolytic mechanism, first yielding a proton and a hydrido-species which again is double-oxidized to release another proton. Three of the four presumed catalytic intermediates (H, H/H and H) were characterized, using various spectroscopic techniques. However, in catalytically active enzyme, the state containing the hydrido-species, which is eponymous for the proposed heterolytic mechanism, has yet only been speculated about. We use different strategies to trap and spectroscopically characterize this transient hydride state (H) for three wild-type [FeFe]-hydrogenases. Applying a novel set-up for real-time attenuated total-reflection Fourier-transform infrared spectroscopy, we monitor compositional changes in the state-specific infrared signatures of [FeFe]-hydrogenases, varying buffer pH and gas composition. We selectively enrich the equilibrium concentration of H, applying Le Chatelier's principle by simultaneously increasing substrate and product concentrations (H/H). Site-directed manipulation, targeting either the proton-transfer pathway or the adt ligand, significantly enhances H accumulation independent of pH. PubMed: 28722011DOI: 10.1038/ncomms16115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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