Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes
Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Camponeschi, Francesca [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019transfer abstract |
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| Umfang: |
9 |
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| Übergeordnetes Werk: |
Enthalten in: Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent - Wang, Yuntao ELSEVIER, 2015, JMB, Amsterdam [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:431 ; year:2019 ; number:22 ; day:8 ; month:11 ; pages:4514-4522 ; extent:9 |
| Links: |
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| DOI / URN: |
10.1016/j.jmb.2019.08.018 |
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| 520 | |a Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. | ||
| 520 | |a Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. | ||
| 700 | 1 | |a Muzzioli, Riccardo |4 oth | |
| 700 | 1 | |a Ciofi-Baffoni, Simone |4 oth | |
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| 700 | 1 | |a Banci, Lucia |4 oth | |
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10.1016/j.jmb.2019.08.018 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000879.pica (DE-627)ELV048612375 (ELSEVIER)S0022-2836(19)30542-X DE-627 ger DE-627 rakwb eng 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Camponeschi, Francesca verfasserin aut Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes 2019transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. Muzzioli, Riccardo oth Ciofi-Baffoni, Simone oth Piccioli, Mario oth Banci, Lucia oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:431 year:2019 number:22 day:8 month:11 pages:4514-4522 extent:9 https://doi.org/10.1016/j.jmb.2019.08.018 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 431 2019 22 8 1108 4514-4522 9 |
| spelling |
10.1016/j.jmb.2019.08.018 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000879.pica (DE-627)ELV048612375 (ELSEVIER)S0022-2836(19)30542-X DE-627 ger DE-627 rakwb eng 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Camponeschi, Francesca verfasserin aut Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes 2019transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. Muzzioli, Riccardo oth Ciofi-Baffoni, Simone oth Piccioli, Mario oth Banci, Lucia oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:431 year:2019 number:22 day:8 month:11 pages:4514-4522 extent:9 https://doi.org/10.1016/j.jmb.2019.08.018 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 431 2019 22 8 1108 4514-4522 9 |
| allfields_unstemmed |
10.1016/j.jmb.2019.08.018 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000879.pica (DE-627)ELV048612375 (ELSEVIER)S0022-2836(19)30542-X DE-627 ger DE-627 rakwb eng 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Camponeschi, Francesca verfasserin aut Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes 2019transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. Muzzioli, Riccardo oth Ciofi-Baffoni, Simone oth Piccioli, Mario oth Banci, Lucia oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:431 year:2019 number:22 day:8 month:11 pages:4514-4522 extent:9 https://doi.org/10.1016/j.jmb.2019.08.018 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 431 2019 22 8 1108 4514-4522 9 |
| allfieldsGer |
10.1016/j.jmb.2019.08.018 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000879.pica (DE-627)ELV048612375 (ELSEVIER)S0022-2836(19)30542-X DE-627 ger DE-627 rakwb eng 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Camponeschi, Francesca verfasserin aut Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes 2019transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. Muzzioli, Riccardo oth Ciofi-Baffoni, Simone oth Piccioli, Mario oth Banci, Lucia oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:431 year:2019 number:22 day:8 month:11 pages:4514-4522 extent:9 https://doi.org/10.1016/j.jmb.2019.08.018 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 431 2019 22 8 1108 4514-4522 9 |
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10.1016/j.jmb.2019.08.018 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000000879.pica (DE-627)ELV048612375 (ELSEVIER)S0022-2836(19)30542-X DE-627 ger DE-627 rakwb eng 540 VZ 660 VZ 540 VZ BIODIV DE-30 fid 42.13 bkl Camponeschi, Francesca verfasserin aut Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes 2019transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. Muzzioli, Riccardo oth Ciofi-Baffoni, Simone oth Piccioli, Mario oth Banci, Lucia oth Enthalten in Elsevier Wang, Yuntao ELSEVIER Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent 2015 JMB Amsterdam [u.a.] (DE-627)ELV012766127 volume:431 year:2019 number:22 day:8 month:11 pages:4514-4522 extent:9 https://doi.org/10.1016/j.jmb.2019.08.018 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-BIODIV SSG-OLC-PHA GBV_ILN_40 42.13 Molekularbiologie VZ AR 431 2019 22 8 1108 4514-4522 9 |
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Enthalten in Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent Amsterdam [u.a.] volume:431 year:2019 number:22 day:8 month:11 pages:4514-4522 extent:9 |
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Enthalten in Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent Amsterdam [u.a.] volume:431 year:2019 number:22 day:8 month:11 pages:4514-4522 extent:9 |
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Fabrication of chitin microspheres and their multipurpose application as catalyst support and adsorbent |
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Camponeschi, Francesca @@aut@@ Muzzioli, Riccardo @@oth@@ Ciofi-Baffoni, Simone @@oth@@ Piccioli, Mario @@oth@@ Banci, Lucia @@oth@@ |
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paramagnetic 1h nmr spectroscopy to investigate the catalytic mechanism of radical s-adenosylmethionine enzymes |
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Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes |
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Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. |
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Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. |
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Iron–sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that 1H NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. 1H NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. |
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Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes |
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