13 C-NMR study of labeled vinyl groups in paramagnetic myoglobin derivatives
The 13C-NMR spectra of high-spin met-aquo myoglobin, spin-equilibrium met-azido myoglobin, low-spin met-cyano myoglobin, deoxy myoglobin and carbonmonoxy myoglobin from sperm whale reconstituted with hemin 13C enriched at both vinyl α or β positions have been recorded. In all cases the labeled vinyl...
| Published in: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology |
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| Main Authors: | , , , |
| Format: | Text |
| Language: | unknown |
| Published: |
LSU Digital Commons
1987
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| Subjects: | |
| Online Access: | https://digitalcommons.lsu.edu/chemistry_pubs/1980 https://doi.org/10.1016/0167-4838(87)90092-6 |
| Summary: | The 13C-NMR spectra of high-spin met-aquo myoglobin, spin-equilibrium met-azido myoglobin, low-spin met-cyano myoglobin, deoxy myoglobin and carbonmonoxy myoglobin from sperm whale reconstituted with hemin 13C enriched at both vinyl α or β positions have been recorded. In all cases the labeled vinyl 13C signals are clearly resolved and useful spectra could be obtained within approx. 15 minutes. The decoupling of multiplet structure due to attached proton(s) has led to the specific assignment of vinyl 13Cα signals in all paramagnetic derivatives and the 13Cβ signals in met-cyano myoglobin. In all other cases, the collapse of the proton multiplet structure as a function of 1H decoupling frequency has located, but not assigned, the attached 1H resonance positions which are obscured by the intense diamagnetic envelope in the 1H-NMR spectrum. The resulting vinyl 13C hyperfine shifts follow Curie behavior, and the patterns closely resemble those in the appropriate model complexes in the same oxidation/spin/ligation state, except that the protein exhibits more in-plane asymmetry. The hyperfine shift patterns are indicative of dominant π contact shifts for all ferric complexes. Deoxy myoglobin vinyl 13C and 1H contact shifts provide little evidence for π bonding. © 1987. |
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