6NAC
Crystal structure of [FeFe]-hydrogenase I (CpI) solved with single pulse free electron laser data
Summary for 6NAC
| Entry DOI | 10.2210/pdb6nac/pdb |
| Related | 6N59 6N6P |
| 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 | [fefe]-hydrogenase, reactivity of [fefe]-hydrogenase, clostridium pasteurianum, iron sulfur clusters, electron-transfer, catalysis, oxidoreductase |
| Biological source | Clostridium pasteurianum |
| Total number of polymer chains | 1 |
| Total formula weight | 66032.62 |
| Authors | Cohen, A.E.,Davidson, C.M.,Zadvornyy, O.A.,Keable, S.M.,Lyubimov, A.Y.,Song, J.,McPhillips, S.E.,Soltis, S.M.,Peters, J.W. (deposition date: 2018-12-05, release date: 2019-12-11, Last modification date: 2023-10-11) |
| Primary citation | Artz, J.H.,Zadvornyy, O.A.,Mulder, D.W.,Keable, S.M.,Cohen, A.E.,Ratzloff, M.W.,Williams, S.G.,Ginovska, B.,Kumar, N.,Song, J.,McPhillips, S.E.,Davidson, C.M.,Lyubimov, A.Y.,Pence, N.,Schut, G.J.,Jones, A.K.,Soltis, S.M.,Adams, M.W.W.,Raugei, S.,King, P.W.,Peters, J.W. Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases. J.Am.Chem.Soc., 142:1227-1235, 2020 Cited by PubMed Abstract: Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interactions of the iron-sulfur-containing catalytic site with the local protein environment are thought to contribute to differences in catalytic reactivity, but this has not been demonstrated. The microbe produces three [FeFe]-hydrogenases that differ in "catalytic bias" by exerting a disproportionate rate acceleration in one direction or the other that spans a remarkable 6 orders of magnitude. The combination of high-resolution structural work, biochemical analyses, and computational modeling indicates that protein secondary interactions directly influence the relative stabilization/destabilization of different oxidation states of the active site metal cluster. This selective stabilization or destabilization of oxidation states can preferentially promote hydrogen oxidation or proton reduction and represents a simple yet elegant model by which a protein catalytic site can confer catalytic bias. PubMed: 31816235DOI: 10.1021/jacs.9b08756 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
Download full validation report
