Unique cyanide nitrogen-15 nuclear magnetic resonance chemical shift values for cyano-peroxidase complexes. Relevance to the heme active-site structure and mechanism of peroxide activation
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference25 articles.
1. Carbon-13 nuclear magnetic resonance spectroscopy of iron(III) porphyrin-cyanide complexes. Location of the bound cyanide ion resonance
2. NMR studies of the binding of 15 N-labeled ligands to hemoproteins pH-Dependent features of heme-bound C15 N-resonances in cyanide complexes of myoglobin and cytochrome c and some implications for their heme environmental structures
3. Nuclear magnetic resonance studies of the binding of15N-labelled ligands to haemins and haemoproteins. Solvent effects on the15N paramagnetic shifts of iron–bound C15N–in low–spin haemin cyanide complexes and cyano haemoproteins
4. 15N magnetic resonance studies of the binding of 15N-labeled cyanide to various hemoproteins
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