Spermine binding to liver mitochondria deenergized by ruthenium red plus either FCCP or antimycin A

FEBS Letters

Dalla Via, Lisa¹  Di Noto, Vito²  Toninello, Antonio³ 

[1] Dipartimento di Scienze Farmaceutiche, Università di Padova, via Marzolo 5, 35121 Padua, Italy;Dipartimento di Chimica Inorganica, Metallorganica ed Analitica, Università di Padova, via Loredan 4, 35121 Padua, Italy;Dipartimento di Chimica Biologica, Università di Padova, Centro di Studio delle Biomembrane del CNR di Padova, viale G. Colombo 3, 35121 Padua, Italy

关键词: Spermine;    Binding site;    Deenergized mitochondrion;    Permeability transition;   

DOI  :  10.1016/S0014-5793(97)01594-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Thermodynamic analysis of spermine binding to mitochondria treated with ruthenium red and deenergized with either FCCP or antimycin A confirms the presence of two polyamine binding sites, S₁ and S₂, both with monocoordination, as previously observed in energized mitochondria [Dalla Via et al., Biochim. Biophys. Acta 1284 (1996) 247–252]. Both sites undergo a marked change in binding capacity and binding affinity upon mitochondrial deenergization. This change is most likely responsible for the incomplete or delayed spermine-mediated inhibition of the permeability transition induced in deenergized mitochondria.

【 授权许可】

Unknown