8BHX
High resolution structure of the iron Superoxide Dismutase from Thermobifida fusca
Summary for 8BHX
| Entry DOI | 10.2210/pdb8bhx/pdb |
| Descriptor | Superoxide dismutase, FE (III) ION, BORIC ACID, ... (4 entities in total) |
| Functional Keywords | iron superoxide dismutase, sod, thermobifida fusca, thermophilic bacteria, reactive oxygen species (ros)., electron transport |
| Biological source | Thermobifida fusca |
| Total number of polymer chains | 2 |
| Total formula weight | 45654.55 |
| Authors | Leiros, H.-K.S.,Sorlie, M. (deposition date: 2022-11-01, release date: 2023-09-27, Last modification date: 2023-10-04) |
| Primary citation | Hamre, A.G.,Al-Sadawi, R.,Johannesen, K.M.,Bisarro, B.,Kjendseth, A.R.,Leiros, H.S.,Sorlie, M. Initial characterization of an iron superoxide dismutase from Thermobifida fusca. J.Biol.Inorg.Chem., 28:689-698, 2023 Cited by PubMed Abstract: Superoxide dismutases (SODs) are enzymes that catalyze the dismutation of the superoxide radical anion into O and HO in a two-step reaction. They are ubiquitous to all forms of life and four different types of metal centers are detected, dividing this class of enzymes into Cu-/Zn-, Ni-, Mn-, and Fe-SODs. In this study, a superoxide dismutase from the thermophilic bacteria Thermobifida fusca (TfSOD) was cloned and expressed before the recombinant enzyme was characterized. The enzyme was found to be active for superoxide dismutation measured by inhibition of cytochrome c oxidation and the inhibition of the autoxidation of pyrogallol. Its pH-optimum was determined to be 7.5, while it has a broad temperature optimum ranging from 20 to 90 °C. Combined with the T that was found to be 78.5 ± 0.5 °C at pH 8.0, TfSOD can be defined as a thermostable enzyme. Moreover, the crystal structure of TfSOD was determined and refined to 1.25 Å resolution. With electron paramagnetic resonance spectroscopy, it was confirmed that iron is the metal co-factor of TfSOD. The cell potential (E) for the TfSOD-Fe/TfSOD-Fe redox couple was determined to be 287 mV. PubMed: 37725277DOI: 10.1007/s00775-023-02019-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
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