Interaction of an anticancer ruthenium complex HInd[RuInd2CI4] with cytochrome C

• Autorzy: Trynda-Lemiesz L.
• Języki publikacji: EN

Abstrakty

EN

Cytochrome c is an important electron transfer protein in the respiratory chain, shuttling electrons from cytochrome c reductase to cytochrome c oxidase. Extensive chemical modification studies indicate significant electrostatic interactions between these proteins and show that all structural and conformational changes of cytochrome c can influence the electron transport. In the present work we examine the effect of an anticancer ruthenium complex, trans-Indazolium (bisindazole) tetra- chlororuthenate(III) (HInd[RuInd2Cl4]), on the conformation of cytochrome c, the state of the heme moiety, formation of the protein dimer and on the folding state of apocytochrome c. For this purpose, gel-filtration chromatography, absorption sec­ond derivative spectroscopy, circular dichroism (CD) and inductively coupled plasma atomic emission spectroscopy (ICP(AES)) were used. The present data have revealed that binding of the potential anticancer drug HInd[RuInd2Cl4] complex to cytochrome c induces a conformation of the protein with less organized secondary and tertiary structure.

Słowa kluczowe

EN

cytochrome C reductase; cytochrome C; chemical modification; respiratory chain; interaction; electrostatic interaction; electron transfer protein; anticancer ruthenium complex; protein; ruthenium; cytochrome C oxidase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2004
• Tom: 51
• Numer: 1
• Opis fizyczny: p.199-205,fig.,ref.

Twórcy

autor

Trynda-Lemiesz L.

• University of Wroclaw, F.Joliot-Curie 14, 50-383 Wroclaw, Poland

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