Gouri Shankar Pandey, Chen Yanover, et al.
PLoS Computational Biology
Paper
NMR double resonance study of azidoferricytochrome c
Abstract
An NMR double resonance study of a mixture of ferricytochrome c and azidoferricytochrome c reveals the presence of an exchange of azide ions between the protein molecules. Irradiation of one of the several resolved methyl resonances from ferricytochrome c cross saturates a correspondingly unique resonance of azidoferricytochrome c and vice versa. The hyperfine shifted resonances of azidoferricytochrome c are thus correlated with those of ferricytochrome c and assigned to porphyrin ring methyls. "On-Off" rates for the azide ion are determined. © 1970.
Related
Laxmi Parida, Pier F. Palamara, et al.
BMC Bioinformatics
Alice Driessen, Susane Unger, et al.
ISMB 2023
Toby G. Rossman, Ekaterina I. Goncharova, et al.
Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis