Electron paramagnetic resonance studies of highly anisotropic low-spin states of ferrimyoglobin derivatives.
Biochim Biophys Acta
; 743(2): 290-8, 1983 Mar 16.
Article
em En
| MEDLINE
| ID: mdl-6297601
ABSTRACT
The effects of addition of nitrogenous bases, which gave low-spin ferric porphyrin complexes with highly anisotropic g values, were investigated for ferrimyoglobin by low-temperature EPR measurements. Concomitant denaturation of myoglobin upon addition of the exogenous bases was also of interest. By addition of pyridine-type bases under regulated pH, Mb(Fe3+) complexes showing EPR spectra with highly anisotropic g values were formed. These complexes have the electronic states close to the spin-crossover point but not so close as that of the ferric porphyrin highly anisotropic low-spin (HALS) complexes previously reported. Several types of low-spin species, LSi, LSa and LSb, were produced by the denaturation of myoglobin caused by addition of some exogenous ligands. The LSi was assigned to a complex with histidine-E7 coordinated on the sixth position and LSa to the one with OH- and histidine-F8[Im0].
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Base de dados:
MEDLINE
Assunto principal:
Hemeproteínas
/
Metamioglobina
Idioma:
En
Ano de publicação:
1983
Tipo de documento:
Article