Two models have been proposed to explain the interaction of cytochrome c with cardiolipin (CL) vesicles. In one case, an acyl chain of the phospholipid accommodates into a hydrophobic channel of the protein located close the Asn52 residue, whereas the alternative model considers the insertion of the acyl chain in the region of the Met80-containing loop. In an attempt to clarify which proposal offers a more appropriate explanation of cytochrome c-CL binding, we have undertaken a spectroscopic and kinetic study of the wild type and the Asn52Ile mutant of iso-1-cytochrome c from yeast to investigate the interaction of cytochrome c with CL vesicles, considered here a model for the CL-containing mitochondrial membrane. Replacement of Asn52, an invariant residue located in a small helix segment of the protein, may provide data useful to gain novel information on which region of cytochrome c is involved in the binding reaction with CL vesicles. In agreement with our recent results revealing that two distinct transitions take place in the cytochrome c-CL binding reaction, data obtained here support a model in which two (instead of one, as considered so far) adjacent acyl chains of the liposome are inserted, one at each of the hydrophobic sites, into the same cytochrome c molecule to form the cytochrome c-CL complex.

Sinibaldi, F., Howes, B., Piro, M.c., Polticelli, F., Bombelli, C., Ferri, T., et al. (2010). Extended cardiolipin anchorage to cytochrome c: model for protein-mitochondrial membrane binding. JBIC, 15(5), 689-700 [10.1007/s00775-010-0636-z].

Extended cardiolipin anchorage to cytochrome c: model for protein-mitochondrial membrane binding.

SINIBALDI, FEDERICA;PIRO, MARIA CRISTINA;COLETTA, MASSIMILIANO;SANTUCCI, ROBERTO
2010

Abstract

Two models have been proposed to explain the interaction of cytochrome c with cardiolipin (CL) vesicles. In one case, an acyl chain of the phospholipid accommodates into a hydrophobic channel of the protein located close the Asn52 residue, whereas the alternative model considers the insertion of the acyl chain in the region of the Met80-containing loop. In an attempt to clarify which proposal offers a more appropriate explanation of cytochrome c-CL binding, we have undertaken a spectroscopic and kinetic study of the wild type and the Asn52Ile mutant of iso-1-cytochrome c from yeast to investigate the interaction of cytochrome c with CL vesicles, considered here a model for the CL-containing mitochondrial membrane. Replacement of Asn52, an invariant residue located in a small helix segment of the protein, may provide data useful to gain novel information on which region of cytochrome c is involved in the binding reaction with CL vesicles. In agreement with our recent results revealing that two distinct transitions take place in the cytochrome c-CL binding reaction, data obtained here support a model in which two (instead of one, as considered so far) adjacent acyl chains of the liposome are inserted, one at each of the hydrophobic sites, into the same cytochrome c molecule to form the cytochrome c-CL complex.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10
English
Con Impact Factor ISI
Models, Molecular; Kinetics; Cytochromes c; Cardiolipins; Mitochondrial Membranes; Binding Sites
Sinibaldi, F., Howes, B., Piro, M.c., Polticelli, F., Bombelli, C., Ferri, T., et al. (2010). Extended cardiolipin anchorage to cytochrome c: model for protein-mitochondrial membrane binding. JBIC, 15(5), 689-700 [10.1007/s00775-010-0636-z].
Sinibaldi, F; Howes, B; Piro, Mc; Polticelli, F; Bombelli, C; Ferri, T; Coletta, M; Smulevich, G; Santucci, R
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/39728
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