Structural characterization of lactoperoxidase in the heme environment by proton NMR spectroscopy
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00368a002
Reference49 articles.
1. Antonini, E. & Brunori, M. (1971) in Hemoglobin and Myoglobin in Their Reaction with Ligands, pp40-50, North-Holland, Amsterdam.
2. 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
3. Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes
4. Proton NMR study of the deprotonation of axial imidazole ligands in low-spin ferric porphyrin complexes
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3. Resonance Raman Evidence for Protein-Induced Out-of-Plane Distortion of the Heme Prosthetic Group of Mammalian Lactoperoxidase;Journal of the American Chemical Society;2002-05-15
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