Thomas Zimmerman, Vito P. Pastore, et al.
arXiv
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.
Thomas Zimmerman, Vito P. Pastore, et al.
arXiv
T.C. Rodman, B.J. Flehinger, et al.
Cytogenetics and Cell Genetics
Ella Barkan, Ibrahim Siddiqui, et al.
Computational And Structural Biotechnology Journal
Eran Eden, Doron Lipson, et al.
PLoS Computational Biology