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NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | FEBS Letters, 591, 2017, 12, S. 1657-1666 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Dantas, Joana M. Brausemann, Anton Einsle, Oliver Salgueiro, Carlos A. Dantas, Joana M. Brausemann, Anton Einsle, Oliver Salgueiro, Carlos A. |
|---|---|
| author |
Dantas, Joana M. Brausemann, Anton Einsle, Oliver Salgueiro, Carlos A. |
| spellingShingle |
Dantas, Joana M. Brausemann, Anton Einsle, Oliver Salgueiro, Carlos A. FEBS Letters NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
dantas, joana m. |
| spelling |
Dantas, Joana M. Brausemann, Anton Einsle, Oliver Salgueiro, Carlos A. 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1002/1873-3468.12695 <jats:p><jats:italic>Geobacter sulfurreducens</jats:italic> is a dissimilatory metal‐reducing bacterium with notable properties and significance in biotechnological applications. Biochemical studies suggest that the inner membrane‐associated diheme cytochrome MacA and the periplasmic triheme cytochrome PpcA from <jats:italic>G. sulfurreducens</jats:italic> can exchange electrons. In this work, NMR chemical shift perturbation measurements were used to map the interface region and to measure the binding affinity between PpcA and MacA. The results show that MacA binds to PpcA in a cleft defined by hemes I and IV, favoring the contact between PpcA heme IV and the MacA high‐potential heme. The dissociation constant values indicate the formation of a low‐affinity complex between the proteins, which is consistent with the transient interaction observed in electron transfer complexes.</jats:p> NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from <i>Geobacter sulfurreducens</i> FEBS Letters |
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Wiley, 2017 |
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| title |
NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_unstemmed |
NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_full |
NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_fullStr |
NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_full_unstemmed |
NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_short |
NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_sort |
nmr studies of the interaction between inner membrane‐associated and periplasmic cytochromes from <i>geobacter sulfurreducens</i> |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1002/1873-3468.12695 |
| publishDate |
2017 |
| physical |
1657-1666 |
| description |
<jats:p><jats:italic>Geobacter sulfurreducens</jats:italic> is a dissimilatory metal‐reducing bacterium with notable properties and significance in biotechnological applications. Biochemical studies suggest that the inner membrane‐associated diheme cytochrome MacA and the periplasmic triheme cytochrome PpcA from <jats:italic>G. sulfurreducens</jats:italic> can exchange electrons. In this work, NMR chemical shift perturbation measurements were used to map the interface region and to measure the binding affinity between PpcA and MacA. The results show that MacA binds to PpcA in a cleft defined by hemes I and IV, favoring the contact between PpcA heme IV and the MacA high‐potential heme. The dissociation constant values indicate the formation of a low‐affinity complex between the proteins, which is consistent with the transient interaction observed in electron transfer complexes.</jats:p> |
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| author | Dantas, Joana M., Brausemann, Anton, Einsle, Oliver, Salgueiro, Carlos A. |
| author_facet | Dantas, Joana M., Brausemann, Anton, Einsle, Oliver, Salgueiro, Carlos A., Dantas, Joana M., Brausemann, Anton, Einsle, Oliver, Salgueiro, Carlos A. |
| author_sort | dantas, joana m. |
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| description | <jats:p><jats:italic>Geobacter sulfurreducens</jats:italic> is a dissimilatory metal‐reducing bacterium with notable properties and significance in biotechnological applications. Biochemical studies suggest that the inner membrane‐associated diheme cytochrome MacA and the periplasmic triheme cytochrome PpcA from <jats:italic>G. sulfurreducens</jats:italic> can exchange electrons. In this work, NMR chemical shift perturbation measurements were used to map the interface region and to measure the binding affinity between PpcA and MacA. The results show that MacA binds to PpcA in a cleft defined by hemes I and IV, favoring the contact between PpcA heme IV and the MacA high‐potential heme. The dissociation constant values indicate the formation of a low‐affinity complex between the proteins, which is consistent with the transient interaction observed in electron transfer complexes.</jats:p> |
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| spelling | Dantas, Joana M. Brausemann, Anton Einsle, Oliver Salgueiro, Carlos A. 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1002/1873-3468.12695 <jats:p><jats:italic>Geobacter sulfurreducens</jats:italic> is a dissimilatory metal‐reducing bacterium with notable properties and significance in biotechnological applications. Biochemical studies suggest that the inner membrane‐associated diheme cytochrome MacA and the periplasmic triheme cytochrome PpcA from <jats:italic>G. sulfurreducens</jats:italic> can exchange electrons. In this work, NMR chemical shift perturbation measurements were used to map the interface region and to measure the binding affinity between PpcA and MacA. The results show that MacA binds to PpcA in a cleft defined by hemes I and IV, favoring the contact between PpcA heme IV and the MacA high‐potential heme. The dissociation constant values indicate the formation of a low‐affinity complex between the proteins, which is consistent with the transient interaction observed in electron transfer complexes.</jats:p> NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from <i>Geobacter sulfurreducens</i> FEBS Letters |
| spellingShingle | Dantas, Joana M., Brausemann, Anton, Einsle, Oliver, Salgueiro, Carlos A., FEBS Letters, NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_full | NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_fullStr | NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_full_unstemmed | NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_short | NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| title_sort | nmr studies of the interaction between inner membrane‐associated and periplasmic cytochromes from <i>geobacter sulfurreducens</i> |
| title_unstemmed | NMR studies of the interaction between inner membrane‐associated and periplasmic cytochromes from Geobacter sulfurreducens |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1002/1873-3468.12695 |