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Issue 35, 2014
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Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR

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Abstract

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.

Graphical abstract: Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR

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Publication details

The article was received on 01 Dec 2013, accepted on 07 Mar 2014 and first published on 07 Mar 2014


Article type: Communication
DOI: 10.1039/C3CC49135H
Citation: Chem. Commun., 2014,50, 4561-4563

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

    S. E. Neto, B. M. Fonseca, C. Maycock and R. O. Louro, Chem. Commun., 2014, 50, 4561
    DOI: 10.1039/C3CC49135H

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