A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
The diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG by combining magnetic resonance, near-IR and Möss...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2019-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-019-09020-4 |
| _version_ | 1818842116860674048 |
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| author | Kimberly Rizzolo Steven E. Cohen Andrew C. Weitz Madeline M. López Muñoz Michael P. Hendrich Catherine L. Drennan Sean J. Elliott |
| author_facet | Kimberly Rizzolo Steven E. Cohen Andrew C. Weitz Madeline M. López Muñoz Michael P. Hendrich Catherine L. Drennan Sean J. Elliott |
| author_sort | Kimberly Rizzolo |
| collection | DOAJ |
| description | The diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG by combining magnetic resonance, near-IR and Mössbauer spectroscopies and electrochemical methods. |
| first_indexed | 2024-12-19T04:36:52Z |
| format | Article |
| id | doaj.art-43e89e2788134c44bc04e90574efd768 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-19T04:36:52Z |
| publishDate | 2019-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-43e89e2788134c44bc04e90574efd7682022-12-21T20:35:43ZengNature PortfolioNature Communications2041-17232019-03-0110111010.1038/s41467-019-09020-4A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) stateKimberly Rizzolo0Steven E. Cohen1Andrew C. Weitz2Madeline M. López Muñoz3Michael P. Hendrich4Catherine L. Drennan5Sean J. Elliott6Boston University, Department of ChemistryMassachusetts Institute of Technology, Department of ChemistryCarnegie Mellon University, Department of ChemistryBoston University, Department of ChemistryCarnegie Mellon University, Department of ChemistryMassachusetts Institute of Technology, Department of ChemistryBoston University, Department of ChemistryThe diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG by combining magnetic resonance, near-IR and Mössbauer spectroscopies and electrochemical methods.https://doi.org/10.1038/s41467-019-09020-4 |
| spellingShingle | Kimberly Rizzolo Steven E. Cohen Andrew C. Weitz Madeline M. López Muñoz Michael P. Hendrich Catherine L. Drennan Sean J. Elliott A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state Nature Communications |
| title | A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state |
| title_full | A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state |
| title_fullStr | A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state |
| title_full_unstemmed | A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state |
| title_short | A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state |
| title_sort | widely distributed diheme enzyme from burkholderia that displays an atypically stable bis fe iv state |
| url | https://doi.org/10.1038/s41467-019-09020-4 |
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