Literature DB >> 9571115

Paramagnetic Inversion of the Sign of the Interference Contribution to the Transverse Relaxation of the Imido Protons of the Coordinated Imidazoles in the Uniformly 15N-Labeled Cytochrome c3

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Abstract

In the spectrum of uniformly 15N-labeled cytochrome c3, the relative linewidths of the doublet peaks of the 15N-coupled imido proton of the coordinated imidazole group were reversed on oxidation. This inversion was explained by the interference relaxation process between the electron-proton dipolar and 15N-1H dipolar interactions. The inversion can be used to assign the imido protons of the coordinated imidazole groups in heme proteins. Copyright 1998 Academic Press.

Entities:  

Year:  1998        PMID: 9571115     DOI: 10.1006/jmre.1998.1378

Source DB:  PubMed          Journal:  J Magn Reson        ISSN: 1090-7807            Impact factor:   2.229


  1 in total

1.  Geometry dependent two-dimensional heteronuclear multiplet effects in paramagnetic proteins.

Authors:  P K Madhu; R Grandori; K Hohenthanner; P K Mandal; N Müller
Journal:  J Biomol NMR       Date:  2001-05       Impact factor: 2.835

  1 in total

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