Assignment of hyperfine shifted haem methyl carbon resonances in paramagnetic low-spin met-cyano complex of sperm whale myoglobin.
FEBS Lett
; 222(1): 115-9, 1987 Sep 28.
Article
em En
| MEDLINE
| ID: mdl-3653391
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 1H-13C 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 degrees 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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Heme
/
Hemeproteínas
/
Metamioglobina
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1987
Tipo de documento:
Article
País de afiliação:
Japão