Evaluation of cytochrome c affinity to anionic phospholipids by means of surface plasmon resonance.
FEBS Lett
; 583(1): 97-100, 2009 Jan 05.
Article
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| MEDLINE
| ID: mdl-19059242
ABSTRACT
We attempted to evaluate the affinity of the anionic phospholipids to cytochrome c by means of surface plasmon resonance (SPR) technique and to correlate it with the cytochrome c active site alterations and peroxidase activity. Our experiments showed a strong interdependence between the phospholipid fatty acid saturation degree, the active site structure alterations and peroxidase activity of the cytochrome c phospholipid complex. Cytochrome c peroxidase activity and Trp59 fluorescence increase in the sequence of phosphatidyl choline (PC)-->phosphatidylserine (PS)-->cardiolipin (CL)-->phosphatidic acid (PA). The association constant (K(a)) increased in the sequence PC-->PA-->PS-->CL. The SPR spectroscopy data shows that K(a) is independent of lipid saturation degree, but correlates with phospholipid negative charge value.
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1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosfolípidos
/
Citocromos c
Idioma:
En
Revista:
FEBS Lett
Año:
2009
Tipo del documento:
Article
País de afiliación:
Rusia