Abstract
The hyperfine shifted resonances arising from all four individual haem carbons of the paramagnetic low-spin met-cyano complex of sperm whale myoglobin have been clearly identified and assigned for the first time with the aid of /sup 1/H-/sup 13/C heteronuclear chemical shift correlated spectroscopy. Alteration of the in-plane symmetry of the electronic structure of haem induced by the ligation of proximal histidyl imidazole spreads the haem carbon resonances to 32 ppm at 22/sup 0/C, indicating the sensitivity of those resonances to the haem electronic/molecular structure. Those resonances are potentially powerful probes in characterizing the nature of haem electronic structure. 25 refs.; 2 figs.; 1 table.
Citation Formats
Yamamoto, Yasuhiko.
Assignment of hyperfine shifted haem methyl carbon resonances in paramagnetic low-spin met-cyano complex of sperm whale myoglobin.
Netherlands: N. p.,
1987.
Web.
doi:10.1016/0014-5793(87)80202-8.
Yamamoto, Yasuhiko.
Assignment of hyperfine shifted haem methyl carbon resonances in paramagnetic low-spin met-cyano complex of sperm whale myoglobin.
Netherlands.
https://doi.org/10.1016/0014-5793(87)80202-8
Yamamoto, Yasuhiko.
1987.
"Assignment of hyperfine shifted haem methyl carbon resonances in paramagnetic low-spin met-cyano complex of sperm whale myoglobin."
Netherlands.
https://doi.org/10.1016/0014-5793(87)80202-8.
@misc{etde_7126146,
title = {Assignment of hyperfine shifted haem methyl carbon resonances in paramagnetic low-spin met-cyano complex of sperm whale myoglobin}
author = {Yamamoto, Yasuhiko}
abstractNote = {The hyperfine shifted resonances arising from all four individual haem carbons of the paramagnetic low-spin met-cyano complex of sperm whale myoglobin have been clearly identified and assigned for the first time with the aid of /sup 1/H-/sup 13/C heteronuclear chemical shift correlated spectroscopy. Alteration of the in-plane symmetry of the electronic structure of haem induced by the ligation of proximal histidyl imidazole spreads the haem carbon resonances to 32 ppm at 22/sup 0/C, indicating the sensitivity of those resonances to the haem electronic/molecular structure. Those resonances are potentially powerful probes in characterizing the nature of haem electronic structure. 25 refs.; 2 figs.; 1 table.}
doi = {10.1016/0014-5793(87)80202-8}
journal = []
volume = {222:1}
journal type = {AC}
place = {Netherlands}
year = {1987}
month = {Sep}
}
title = {Assignment of hyperfine shifted haem methyl carbon resonances in paramagnetic low-spin met-cyano complex of sperm whale myoglobin}
author = {Yamamoto, Yasuhiko}
abstractNote = {The hyperfine shifted resonances arising from all four individual haem carbons of the paramagnetic low-spin met-cyano complex of sperm whale myoglobin have been clearly identified and assigned for the first time with the aid of /sup 1/H-/sup 13/C heteronuclear chemical shift correlated spectroscopy. Alteration of the in-plane symmetry of the electronic structure of haem induced by the ligation of proximal histidyl imidazole spreads the haem carbon resonances to 32 ppm at 22/sup 0/C, indicating the sensitivity of those resonances to the haem electronic/molecular structure. Those resonances are potentially powerful probes in characterizing the nature of haem electronic structure. 25 refs.; 2 figs.; 1 table.}
doi = {10.1016/0014-5793(87)80202-8}
journal = []
volume = {222:1}
journal type = {AC}
place = {Netherlands}
year = {1987}
month = {Sep}
}