Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR

Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR

Residual dipolar couplings measured by NMR spectroscopy reveal that the rhombicity of the electronic structure of low-spin paramagnetic hemes determines their relative contribution to the preferential orientation of a protein with multiple hemes when placed in a strong magnetic field.

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2014-05, Vol.50 (35), p.4561-4563
Hauptverfasser: Neto, S E, Fonseca, B M, Maycock, C, Louro, R O
Format: Artikel
Sprache:eng
Schlagworte:
Alignment
Couplings
Cytochromes
Cytochromes c - chemistry
Electronic structure
Electrons
Heme - chemistry
Magnetic fields
Models, Molecular
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular - methods
Orientation
Protein Conformation
Proteins
Shewanella - chemistry
Shewanella - enzymology
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Beschreibung
Zusammenfassung:Residual dipolar couplings measured by NMR spectroscopy reveal that the rhombicity of the electronic structure of low-spin paramagnetic hemes determines their relative contribution to the preferential orientation of a protein with multiple hemes when placed in a strong magnetic field.
ISSN:1359-7345
1364-548X
DOI:10.1039/c3cc49135h