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<TEX>$^{13}C$</TEX> NMR Analysis for the Characterization of Heme Electronic/Molecular Structure in Horse Myoglobin Cyanide
Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985
1998, v.11 no.1, pp.73-78
Lee,
K., Kweon,
J., Lee,
H., Kim,
Y., &
Choi,
Y.
(1998). <TEX>$^{13}C$</TEX> NMR Analysis for the Characterization of Heme Electronic/Molecular Structure in Horse Myoglobin Cyanide. Analytical Science and Technology, 11(1), 73-78.
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Abstract
The reverse detection heteronuclear multiple quantum coherence, HMQC study of metcyano complex of horse myoglobin(MbCN) has provided the complete assignment of hyperfine shifted resonances of heme carbons attached with proton(s). The application of HMQC experiment to the paramagnetic low-spin MbCN gives clear <TEX>$^1H$</TEX> and <TEX>$^{13}C$</TEX> coherences for the paramagnetic amino acid residues as well as heme side chains, and can be extended to the low-spin paramagnetic hemoprotein derivative for the assignment of natural abundance <TEX>$^{13}C$</TEX> resonances. This assignment strategy can avoid possible ambiguities that may result from the sole utilization of <TEX>$^1H$</TEX> nuclear Overhauser effect for the assignment of heme <TEX>$^1H$</TEX> signals resonating in the diamagnetic region. The resulting 2,4-vinyl <TEX>${\alpha}$</TEX>-carbons and 7-propionate <TEX>${\beta}$</TEX>-carbon follow anomalous anti-Curie behavior, and are indicative of incoplanarity with heme plane. Magnetic/electronic asymmetry of heme induced by proximal histidine(His) makes spread that the hyperfine shifted heme carbon resonances over the range of 250 ppm at <TEX>$25^{\circ}C$</TEX>. These heme carbon resonances would be the much more sensitive probe than those of proton resonances in analyzing the nature of heme electronic structure of myoglobin.
- keywords
- <TEX>$^{13}C$</TEX> NMR, HMQC, myoglohin, heme, hyperfine-shift
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