Nanodisc reconstitution of flavin mononucleotide binding domain of cytochrome-P450-reductase enables high-resolution NMR probing
Cytochrome-P450-reductase transfers electrons to cytochrome-P450 through its flavin mononucleotide binding domain (FBD). Despite the importance of membrane-anchoring for FBD function, studies have focused on its soluble domain lacking the transmembrane-domain. Here we demonstrate that the reconstitu...
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| Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2021-05, Vol.57 (39), p.4819-4822 |
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| container_title | Chemical communications (Cambridge, England) |
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| creator | Krishnarjuna, Bankala Yamazaki, Toshio Anantharamaiah, G. M Ramamoorthy, Ayyalusamy |
| description | Cytochrome-P450-reductase transfers electrons to cytochrome-P450 through its flavin mononucleotide binding domain (FBD). Despite the importance of membrane-anchoring for FBD function, studies have focused on its soluble domain lacking the transmembrane-domain. Here we demonstrate that the reconstitution of FBD in nanodiscs enables high-resolution NMR measurements and renders a stable conformation.
Reconstitution of the flavin mononucleotide binding domain of cyt-P450-reductase in peptide-lipid-nanodiscs provided a stable conformation that assisted in mapping transient lipid-protein interactions and line broadening through chemical shift analysis. |
| doi_str_mv | 10.1039/d1cc01018b |
| format | Article |
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| subjects | Binding Binding Sites Chemistry Chemistry, Multidisciplinary Cytochrome Cytochromes Domains Electron Transport Flavin Mononucleotide - chemistry Flavin Mononucleotide - metabolism High resolution Models, Molecular NADPH-Ferrihemoprotein Reductase - chemistry NADPH-Ferrihemoprotein Reductase - metabolism NMR Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Physical Sciences Reductases Science & Technology |
| title | Nanodisc reconstitution of flavin mononucleotide binding domain of cytochrome-P450-reductase enables high-resolution NMR probing |
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