Sperm whale metMb

Fig. 8. The 400 MHz H NMR spectrum of sperm whale metMb(OH ) in 90%H20/10% H20, pH 9.47, at 5 °C. In the inset, the high-frequency shifted portion, 10-15 ppm, of the spectrum (lower) is expanded, together with the corresponding portion of the spectrum in 100% H2O (upper).

The pH dependence of the high-frequency shifted portions of the 400 MHz H NMR spectra of sperm whale metMb(OH ) is illustrated in Fig. 12A. The... 

Fig. 18. The high-frequency shifted portions of the 400 MHz H NMR spectra of sperm whale metMb(OH ) and apoMb in 90%H20/10%-H20 at 5 °C and neutral (left) and basic (right) pH values. Peak indicated by an asterisk is due to impurity. The preparation of apoMb from Mb is schematically represented in the inset.

Fig. 22. (A) The high-frequency shifted portions, 16-29 ppm, of the 400 MHz H NMR spectra of freshly reconstituted sperm whale metMb(CN ) with protohemin (bottom trace) and native metMb(CN ) (top trace) in 90%H20/10%2H20, pH 9.57, at 25 °C. The signal assignments are given with the spectra. Peaks indicated by an arrow arise from the minor form (B of Fig. 19). (B) and (C) the time evolution of the spectra of freshly reconstituted sperm whale metMb with protohemin in 90%H20/10% H20, pH 7.32, at 5 °C. (B) shows the heme 12- and 18-methyl proton signals of the metMb(CN") converted from the reconstituted metMb(OH ), of which the spectrum is illustrated in (C), immediately after the measurement. (C) shows the high-frequency shifted portions, 10-15 ppm, of the 400 MHz H NMR spectra of freshly reconstituted sperm whale metMb with protohemin in 90%H20/10% H20, pH 7.32, at 5 °C, recorded at the elapsed times indicated. The time evolution of the intensity of peak X in (C) resembles that of heme 18-methyl proton signal of the minor form in (B). (From ref. 187, with permission from Elsevier Science.)...

Fig. 25. Temperature dependence of the high-frequency shifted portions of the 400 MHz H NMR spectra of native sperm whale metMb at pH 9.51 (A), metMb reconstituted with mesohemin at pH 9.53 (B), and metMb reconstituted with deuterohemin at pH 9.52 (C). Peaks indicated by are due to impurity. (From ref. 187, with permission from Elsevier Science.)...

Fig. 15. The high-frequency shifted portions of the 400 MHz H NMR spectra of metMb(OH )s in 90%H ,()/10%-H20 at 2 °C (A) sperm whale Mb, pH9.47 (B) horse Mb, pH 10.01 (C) bovine Mb, pH 9.81. The pH of each sample was adjusted to observe HisGHl NgH proton signal with the minimum line width. The signal assignment is indicated in A. The corresponding signals are connected by broken lines.

Fl rel738. Hme-resolvedbitenutydecaysoftrp TintunameUnyo globin (metMb) and trp-7 and trp-14 in sperm whale (S.W.) metmyoglo-bln. Revised from Ref. 121. 

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