Preferences help
enabled [disable] Abstract
Number of results
2004 | 51 | 1 | 199-205
Article title

Interaction of an anticancer ruthenium complex HInd[RuInd2Cl4] with cytochrome c.

Title variants
Languages of publication
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) tetrachlororuthenate(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.
Physical description
  • Babul J, Stellwagen E. (1972) Biochemistry.; 11: 1195-200.
  • Barker PD, Ferguson SJ. (1999) Structure Fold Des.; 7: 281-90.
  • Beaven GH, Chen SH, d'Albis A, Gratzer WB. (1974) Eur J Biochem.; 41: 539-46.
  • Cai J, Yang J, Jones DP. (1998) Biochim Biophys Acta.; 1366: 139-40.
  • Chen J, Kostic MN. (1988) Inorg Chem.; 27: 2682-7.
  • Clarke MJ. (2002) Coord Chem Rev.; 232: 69-93.
  • Depenbrock H, Schmelcher S, Peter R, Keppler BK, Weirich G, Block T, Rastetter J, Hanauske AR. (1997) Eur J Cancer.; 33: 2404-10.
  • Dumount ME, Corin AF, Campbell GA. (1994) Biochemistry.; 33: 7368-78.
  • Dyson HJ, Beattie JK. (1982) J Biol Chem.; 257: 2267-73.
  • Fisher WR, Taniuchi H, Anfinsen CB. (1973) J Biol Chem.; 248: 3188-95.
  • Jiang L, Chen Yu, Tang G, Tang W. (1997) J Inorg Biochem.; 65: 73-7.
  • Keppler BK, Henn M, Juhl UM, Berger MR, Niebl R, Wagner FE. (1989) Prog Clin Biochem Med.; 10: 41- 69.
  • Keppler BK, Berger MR, Heim ME. (1990) Cancer Treat Rev.; 17: 261-77.
  • Klausner RD, van Renswoude J, Ashwell G, et al. (1983) J Biol Chem.; 258: 4715-24.
  • Kratz F, Hartmann M, Keppler BK, Messori L. (1994) J Biol Chem.; 269: 2581-8.
  • Ragone R, Colonna G, Balestrieri C, Servillo L, Irace G. (1984) Biochemistry.; 23: 1871-5.
  • Rankin SE, Watts A, Pinheiro TJT. (1998) Biochemistry.; 37: 12588-95.
  • Smith CA, Sutherland-Smith AJ, Keppler BK, Kratz F, Baker EN. (1996) Biol Inorg Chem.; 1: 424-31.
  • Stellwagen E, Rysavy R, Babul G. (1972) J Biol Chem.; 247: 8074-7.
  • Tian H, Sadoski R, Zhang L, Yu ChA, Yu L, Durham B, Millett F. (2000) J Biol Chem.; 275: 9587-95.
  • Trynda-Lemiesz L, Karaczyn A, Keppler BK, Kozlowski H. (2000) J Inorg Biochem.; 78: 341-6.
  • Yocom KM, Shelton JB, Shelton JR, Schroeder WA, Worosila G, Isied SS, Bordignon E, Gray HB. (1982) Proc Natl Acad Sci U S A.; 79: 7052-5.
Document Type
Publication order reference
YADDA identifier
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.