Assignment of Hyperfine-Shifted Resonances in Low-Spin Forms of Cytochrome c Peroxidase by Reconstitutions with Deuterated Hemins
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
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