By Regula M. Keller, Kurt Wüthrich (auth.), Lawrence J. Berliner, Jacques Reuben (eds.)
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Extra resources for Biological Magnetic Resonance: Volume 3
CH , CH , 80 40 a ppm Figure 12. High-spin ferric iron- porphyrin complex (Fe 3 + , S = 5/2). 1 H NMR spectrum at 100 MHz of a solution of hemin bromide in d 6 -DMSO, T = 27°C. The spectrum corresponds to the d 6 -DMSO complex of ferriprotoporphyrin IX. , 1971). Multiple Irradiation I H NMR Experiments 15 2. USE OF MULTIPLE IRRADIATION IH NMR TECHNIQUES Most of the I H NMR experiments with hemoproteins discussed in two earlier reviews (Wuthrich, 1970,. 1976) were recorded in the continuous-wave mode at a resonance frequency of 220 MHz.
1978). In contrast to the heme-ring methyls, the resonance positions of the two thioether methyls are only little affected by contact coupling. Since pseudo-contact coupling is thus the dominant hyperfine-interaction term, these resonances provide a basis for the determination of the axes of the electronic 9 tensor. The data in Table III then indicate that when going from horse ferricytochrome c to ferricytochrome c-551, the 9 tensor is rotated by approximately 90° about an axis perpendicular to the heme plane.
Multiple Irradiation I H NMR Experiments 15 2. USE OF MULTIPLE IRRADIATION IH NMR TECHNIQUES Most of the I H NMR experiments with hemoproteins discussed in two earlier reviews (Wuthrich, 1970,. 1976) were recorded in the continuous-wave mode at a resonance frequency of 220 MHz. In these spectra the spin-spin coupling fine structure of the resonances was not usually resolved, and hence, even the use of spin decoupling for the identification of the component resonances in the spin systems of individual heme substituents or amino acid side chains (Wuthrich, 1976) was very limited.