Title
Assignment of Hyperfine-Shifted Resonances in Low-Spin Forms of Cytochrome c Peroxidase by Reconstitutions with Deuterated Hemins
Document Type
Article
Publication Date
1-1-1983
Abstract
Proton magnetic resonance assignments of protons from peripheral heme substituents have been carried out for two low-spin forms of cytochrome c peroxidase: CcP-CN and CcP-N3. The assignments were made by reconstituting CcP with six specifically deuterated protohemin IX derivatives. The results indícate that the pattern of unpaired π spin-density delocalization is consistent with an interpretation whereby the source of the rhombic perturbation is the orientation of the proximal histidine's imidazole plane. However, we also present evidence that a specific interaction between pyrrole II and tryptophan 51 affects the observed shift pattern, thereby contributing to the rhombic perturbation. © 1983, American Chemical Society. All rights reserved.
Publication Source (Journal or Book title)
Journal of the American Chemical Society
First Page
2099
Last Page
2104
Recommended Citation
Satterlee, J., Erman, J., LaMar, G., Smith, K., & Langry, K. (1983). Assignment of Hyperfine-Shifted Resonances in Low-Spin Forms of Cytochrome c Peroxidase by Reconstitutions with Deuterated Hemins. Journal of the American Chemical Society, 105 (8), 2099-2104. https://doi.org/10.1021/ja00346a001