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Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4...
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| Zeitschriftentitel: | mBio |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | mBio, 10, 2019, 4 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
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| Schlagwörter: |
| author_facet |
Rettberg, Lee A. Kang, Wonchull Stiebritz, Martin T. Hiller, Caleb J. Lee, Chi Chung Liedtke, Jasper Ribbe, Markus W. Hu, Yilin Rettberg, Lee A. Kang, Wonchull Stiebritz, Martin T. Hiller, Caleb J. Lee, Chi Chung Liedtke, Jasper Ribbe, Markus W. Hu, Yilin |
|---|---|
| author |
Rettberg, Lee A. Kang, Wonchull Stiebritz, Martin T. Hiller, Caleb J. Lee, Chi Chung Liedtke, Jasper Ribbe, Markus W. Hu, Yilin |
| spellingShingle |
Rettberg, Lee A. Kang, Wonchull Stiebritz, Martin T. Hiller, Caleb J. Lee, Chi Chung Liedtke, Jasper Ribbe, Markus W. Hu, Yilin mBio Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster Virology Microbiology |
| author_sort |
rettberg, lee a. |
| spelling |
Rettberg, Lee A. Kang, Wonchull Stiebritz, Martin T. Hiller, Caleb J. Lee, Chi Chung Liedtke, Jasper Ribbe, Markus W. Hu, Yilin 2161-2129 2150-7511 American Society for Microbiology Virology Microbiology http://dx.doi.org/10.1128/mbio.01497-19 <jats:p> This work reports the crystal structure of a previously uncharacterized Fe protein from a methanogenic organism, which provides important insights into the structural properties of the less-characterized, yet highly interesting archaeal nitrogenase enzymes. Moreover, the structure-derived implications for CO <jats:sub>2</jats:sub> capture by a surface-exposed [Fe <jats:sub>4</jats:sub> S <jats:sub>4</jats:sub> ] cluster point to the possibility of developing novel strategies for CO <jats:sub>2</jats:sub> sequestration while providing the initial insights into the unique mechanism of FeS-based CO <jats:sub>2</jats:sub> activation. </jats:p> Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO <sub>2</sub> Capture by a Surface-Exposed [Fe <sub>4</sub> S <sub>4</sub> ] Cluster mBio |
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10.1128/mbio.01497-19 |
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American Society for Microbiology, 2019 |
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American Society for Microbiology, 2019 |
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| title |
Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_unstemmed |
Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_full |
Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_fullStr |
Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_full_unstemmed |
Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_short |
Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_sort |
structural analysis of a nitrogenase iron protein from methanosarcina acetivorans: implications for co
<sub>2</sub>
capture by a surface-exposed [fe
<sub>4</sub>
s
<sub>4</sub>
] cluster |
| topic |
Virology Microbiology |
| url |
http://dx.doi.org/10.1128/mbio.01497-19 |
| publishDate |
2019 |
| physical |
|
| description |
<jats:p>
This work reports the crystal structure of a previously uncharacterized Fe protein from a methanogenic organism, which provides important insights into the structural properties of the less-characterized, yet highly interesting archaeal nitrogenase enzymes. Moreover, the structure-derived implications for CO
<jats:sub>2</jats:sub>
capture by a surface-exposed [Fe
<jats:sub>4</jats:sub>
S
<jats:sub>4</jats:sub>
] cluster point to the possibility of developing novel strategies for CO
<jats:sub>2</jats:sub>
sequestration while providing the initial insights into the unique mechanism of FeS-based CO
<jats:sub>2</jats:sub>
activation.
</jats:p> |
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| author | Rettberg, Lee A., Kang, Wonchull, Stiebritz, Martin T., Hiller, Caleb J., Lee, Chi Chung, Liedtke, Jasper, Ribbe, Markus W., Hu, Yilin |
| author_facet | Rettberg, Lee A., Kang, Wonchull, Stiebritz, Martin T., Hiller, Caleb J., Lee, Chi Chung, Liedtke, Jasper, Ribbe, Markus W., Hu, Yilin, Rettberg, Lee A., Kang, Wonchull, Stiebritz, Martin T., Hiller, Caleb J., Lee, Chi Chung, Liedtke, Jasper, Ribbe, Markus W., Hu, Yilin |
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| description | <jats:p> This work reports the crystal structure of a previously uncharacterized Fe protein from a methanogenic organism, which provides important insights into the structural properties of the less-characterized, yet highly interesting archaeal nitrogenase enzymes. Moreover, the structure-derived implications for CO <jats:sub>2</jats:sub> capture by a surface-exposed [Fe <jats:sub>4</jats:sub> S <jats:sub>4</jats:sub> ] cluster point to the possibility of developing novel strategies for CO <jats:sub>2</jats:sub> sequestration while providing the initial insights into the unique mechanism of FeS-based CO <jats:sub>2</jats:sub> activation. </jats:p> |
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| spelling | Rettberg, Lee A. Kang, Wonchull Stiebritz, Martin T. Hiller, Caleb J. Lee, Chi Chung Liedtke, Jasper Ribbe, Markus W. Hu, Yilin 2161-2129 2150-7511 American Society for Microbiology Virology Microbiology http://dx.doi.org/10.1128/mbio.01497-19 <jats:p> This work reports the crystal structure of a previously uncharacterized Fe protein from a methanogenic organism, which provides important insights into the structural properties of the less-characterized, yet highly interesting archaeal nitrogenase enzymes. Moreover, the structure-derived implications for CO <jats:sub>2</jats:sub> capture by a surface-exposed [Fe <jats:sub>4</jats:sub> S <jats:sub>4</jats:sub> ] cluster point to the possibility of developing novel strategies for CO <jats:sub>2</jats:sub> sequestration while providing the initial insights into the unique mechanism of FeS-based CO <jats:sub>2</jats:sub> activation. </jats:p> Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO <sub>2</sub> Capture by a Surface-Exposed [Fe <sub>4</sub> S <sub>4</sub> ] Cluster mBio |
| spellingShingle | Rettberg, Lee A., Kang, Wonchull, Stiebritz, Martin T., Hiller, Caleb J., Lee, Chi Chung, Liedtke, Jasper, Ribbe, Markus W., Hu, Yilin, mBio, Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster, Virology, Microbiology |
| title | Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_full | Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_fullStr | Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_full_unstemmed | Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_short | Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| title_sort | structural analysis of a nitrogenase iron protein from methanosarcina acetivorans: implications for co <sub>2</sub> capture by a surface-exposed [fe <sub>4</sub> s <sub>4</sub> ] cluster |
| title_unstemmed | Structural Analysis of a Nitrogenase Iron Protein from Methanosarcina acetivorans: Implications for CO 2 Capture by a Surface-Exposed [Fe 4 S 4 ] Cluster |
| topic | Virology, Microbiology |
| url | http://dx.doi.org/10.1128/mbio.01497-19 |