4C3O
Structure and function of an oxygen tolerant NiFe hydrogenase from Salmonella
Summary for 4C3O
| Entry DOI | 10.2210/pdb4c3o/pdb |
| Descriptor | HYDROGENASE-1 LARGE SUBUNIT, HYDROGENASE-1 SMALL SUBUNIT, formyl[bis(hydrocyanato-1kappaC)]ironnickel(Fe-Ni), ... (10 entities in total) |
| Functional Keywords | oxidoreductase, hydrogen metabolism, nife hydrogenase |
| Biological source | SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM STR. LT2 More |
| Total number of polymer chains | 6 |
| Total formula weight | 292380.37 |
| Authors | Bowman, L.,Flanagan, L.,Fyfe, P.K.,Parkin, A.,Hunter, W.N.,Sargent, F. (deposition date: 2013-08-26, release date: 2014-01-29, Last modification date: 2024-11-13) |
| Primary citation | Bowman, L.,Flanagan, L.,Fyfe, P.K.,Parkin, A.,Hunter, W.N.,Sargent, F. How the Structure of the Large Subunit Controls Function in an Oxygen-Tolerant [Nife]-Hydrogenase. Biochem.J., 458:449-, 2014 Cited by PubMed Abstract: Salmonella enterica is an opportunistic pathogen that produces a [NiFe]-hydrogenase under aerobic conditions. In the present study, genetic engineering approaches were used to facilitate isolation of this enzyme, termed Hyd-5. The crystal structure was determined to a resolution of 3.2 Å and the hydro-genase was observed to comprise associated large and small subunits. The structure indicated that His229 from the large subunit was close to the proximal [4Fe-3S] cluster in the small subunit. In addition, His229 was observed to lie close to a buried glutamic acid (Glu73), which is conserved in oxygen-tolerant hydrogenases. His229 and Glu73 of the Hyd-5 large subunit were found to be important in both hydrogen oxidation activity and the oxygen-tolerance mechanism. Substitution of His229 or Glu73 with alanine led to a loss in the ability of Hyd-5 to oxidize hydrogen in air. Furthermore, the H229A variant was found to have lost the overpotential requirement for activity that is always observed with oxygen-tolerant [NiFe]-hydrogenases. It is possible that His229 has a role in stabilizing the super-oxidized form of the proximal cluster in the presence of oxygen, and it is proposed that Glu73could play a supporting role in fine-tuning the chemistry of His229 to enable this function. PubMed: 24428762DOI: 10.1042/BJ20131520 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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