By Regula M. Keller, Kurt Wüthrich (auth.), Lawrence J. Berliner, Jacques Reuben (eds.)
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Additional info for Biological Magnetic Resonance: Volume 3
First, the preirradiation frequency was on one of the meso-proton resonances at the low-field end of the spectrum, which are sufficiently well separated to be irradiated selectively. Figure 22B shows that two resonances with chemical shifts corresponding to heme-c-ring methyl lines appeared in the TOE difference spectrum obtained with irradiation of the highest field meso-proton line. Inspection of the heme structure (Figure 1) then shows that the two lines in Figure 22B must come from the ring methyls 1 and 8, and that the preirradiation was on the meso-proton b.
Additional identifications of aromatic spin systems in hemoproteins have mainly been obtained by spin decoupling and NOEs. In proteins which contain more than one tryptophan, there has not so far been a straightforward way to correlate the corresponding benzenoid and singlet resonances. Compared to diamagnetic nonheme proteins, additional care has to be exercised in the analysis of the aromatic resonances of hemoproteins. 0 ppm contains, after complete exchange of the labile protons (Wuthrich, 1976), exclusively resonances of Phe, Tyr, Trp, and His.
1978). one phenylalanine in each of the proteins.
Biological Magnetic Resonance: Volume 3 by Regula M. Keller, Kurt Wüthrich (auth.), Lawrence J. Berliner, Jacques Reuben (eds.)