Horse heart ferricytochrome c: conformation and heme configuration of low ionic strength acidic forms.
J Protein Chem
; 9(4): 379-87, 1990 Aug.
Article
em En
| MEDLINE
| ID: mdl-2177335
ABSTRACT
Resonance Raman, absorption and circular dichroism spectroscopic studies of the stable forms of horse heart ferricytochrome c in the pH range 6-0.8 and at the lowest possible ionic strengths, in water, and at 30 degrees C are reported. The neutral pH form, state III, changes to the acidic pH form, state I, through a three-step process state III in equilibrium with IIIa in equilibrium with state II in equilibrium with state I, with pKa's of 3.6 +/- 0.3, 2.7 +/- 0.2, and 1.2 +/- 0.2, depending on the monitoring probe, respectively. State IIIa ferricytochrome c is like state III (i.e., with the Met-80-sulfur-iron linkage and a closed heme crevice) but with a higher degree of folding and a slightly larger porphyrin core. State II ferricytochrome c is an unfolded form with an open heme crevice and no Met-80-sulfur-iron linkage. The heme iron is high-spin, and hexacoordinated with weak ligand-field groups, water, and nitrogen of the protonated/hydrogen-bonded imidazole of the His-18 residue at the axial positions. The state I form also lacks the Met-80-sulfur-iron linkage and has an open heme crevice like the state II form; however, it is less unfolded and has a high-spin pentacoordinated heme iron, with the nitrogen of the imidazole of His-18 as the axial ligate, which is out of the porphyrin plane by about 0.45 A.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Grupo dos Citocromos c
/
Heme
/
Cavalos
/
Miocárdio
Limite:
Animals
Idioma:
En
Revista:
J Protein Chem
Ano de publicação:
1990
Tipo de documento:
Article