Anne Grethe Hamre, Rim Al-Sadawi, Kirsti Merete Johannesen, Bastien Bisarro, Åsmund Røhr Kjendseth, Hanna-Kirsti S. Leiros, Morten Sørlie
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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 <i>T</i><sub>m</sub> that was found to be 78.5 ± 0.5 °C at pH 8.0, <i>Tf</i>SOD can be defined as a thermostable enzyme. Moreover, the crystal structure of <i>Tf</i>SOD 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 <i>Tf</i>SOD. The cell potential (<i>E</i><sub>m</sub>) for the TfSOD-Fe<sup>3+</sup>/TfSOD-Fe<sup>2+</sup> redox couple was determined to be 287 mV.</p><h3>Graphical abstract</h3>\n <figure><div><div><div><picture><source><img></source></picture></div></div></div></figure>\n </div>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"28 7","pages":"689 - 698"},"PeriodicalIF":2.7000,"publicationDate":"2023-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-023-02019-9.pdf","citationCount":"0","resultStr":"{\"title\":\"Initial characterization of an iron superoxide dismutase from Thermobifida fusca\",\"authors\":\"Anne Grethe Hamre, Rim Al-Sadawi, Kirsti Merete Johannesen, Bastien Bisarro, Åsmund Røhr Kjendseth, Hanna-Kirsti S. Leiros, Morten Sørlie\",\"doi\":\"10.1007/s00775-023-02019-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Superoxide dismutases (SODs) are enzymes that catalyze the dismutation of the superoxide radical anion into O<sub>2</sub> and H<sub>2</sub>O<sub>2</sub> 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 <i>Thermobifida fusca</i> (<i>Tf</i>SOD) 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 <i>c</i> 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 <i>T</i><sub>m</sub> that was found to be 78.5 ± 0.5 °C at pH 8.0, <i>Tf</i>SOD can be defined as a thermostable enzyme. Moreover, the crystal structure of <i>Tf</i>SOD 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 <i>Tf</i>SOD. The cell potential (<i>E</i><sub>m</sub>) for the TfSOD-Fe<sup>3+</sup>/TfSOD-Fe<sup>2+</sup> redox couple was determined to be 287 mV.</p><h3>Graphical abstract</h3>\\n <figure><div><div><div><picture><source><img></source></picture></div></div></div></figure>\\n </div>\",\"PeriodicalId\":603,\"journal\":{\"name\":\"JBIC Journal of Biological Inorganic Chemistry\",\"volume\":\"28 7\",\"pages\":\"689 - 698\"},\"PeriodicalIF\":2.7000,\"publicationDate\":\"2023-09-19\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://link.springer.com/content/pdf/10.1007/s00775-023-02019-9.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"JBIC Journal of Biological Inorganic Chemistry\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s00775-023-02019-9\",\"RegionNum\":3,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"JBIC Journal of Biological Inorganic Chemistry","FirstCategoryId":"1","ListUrlMain":"https://link.springer.com/article/10.1007/s00775-023-02019-9","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Initial characterization of an iron superoxide dismutase from Thermobifida fusca
Superoxide dismutases (SODs) are enzymes that catalyze the dismutation of the superoxide radical anion into O2 and H2O2 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 Tm 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 (Em) for the TfSOD-Fe3+/TfSOD-Fe2+ redox couple was determined to be 287 mV.
期刊介绍：
Biological inorganic chemistry is a growing field of science that embraces the principles of biology and inorganic chemistry and impacts other fields ranging from medicine to the environment. JBIC (Journal of Biological Inorganic Chemistry) seeks to promote this field internationally. The Journal is primarily concerned with advances in understanding the role of metal ions within a biological matrix—be it a protein, DNA/RNA, or a cell, as well as appropriate model studies. Manuscripts describing high-quality original research on the above topics in English are invited for submission to this Journal. The Journal publishes original articles, minireviews, and commentaries on debated issues.
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