| Literature DB >> 9571115 |
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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