Electron-transfer-mediated binding of optically active cobalt (III) complexes to horse heart cytochrome c

Journal of the Royal Society Interface

Volumn 2, Issue 2, 2005, Pages 109-112

  Scholten, Ulrich ^a   Merchán, Alejandro Castillejo ^a   Bernauer, Klaus ^a  

^a UNIVERSITY OF NEUCHÂTEL   (Switzerland)

Author keywords

Circular dichroism; Cobalt complexes; Cytochrome c; Electron transfer; Stereoselectivity

Indexed keywords

COBALT; CYTOCHROME C;

ANIMAL; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; ELECTRON TRANSPORT; HEART MUSCLE; HORSE; METABOLISM; PROTEIN BINDING;

ANIMALS; CIRCULAR DICHROISM; COBALT; CYTOCHROMES C; ELECTRON TRANSPORT; HORSES; MYOCARDIUM; PROTEIN BINDING;

EID: 33746883920     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2004.0023     Document Type: Article

References (31)

1. Ahmed, A. J. & Millett, F. 1981 Use of specific lysine modifications to identify the site of reaction between cytochrome c and ferricyanide. J. Biol. Chem. 256, 1611-1615.
2. 2+ complexes. J. Chem. Soc. Dalton Trans. 755-758.
3. Bernauer, K. & Jauslin, P. 1993 Chiral recognition and stereoselective reduction of horse ferricytochrome c by optically active iron(II) complexes. Chimia 47, 218-220.
4. Bernauer, K. & Pousaz, P. 1984 Stereoselective formation of cobalt (III) complexes with new linear pentadentate ligands. Helv. Chim. Acta 67, 796-803.
5. Bernauer, K. & Sauvain, J. J. 1988 Stereoselectivity in the reaction of spinach plastocyanin with optically active reducing agents. J. Chem. Soc. Chem. Commun. 353-354.
6. + and optically active iron(II) complexes. Helv. Chim. Acta 71, 1339.
7. Bernauer, K., Monzione, M., Schürmann, P. & Viette, V. 1990 Stereoselectivity and chiral recognition in the electron-transfer reaction between spinach ferredoxin and optically active cobalt(III) complexes. Helv. Chim. Acta 73, 346-352.
8. Bernauer, K., Sclmrmann, P., Nusbaumer, C., Verardo, L. & Ghizdavu, S. 1998 Stereo- and site selection by enantiomers in electron-transfer reactions involving native and recombinant metalloproteins. J. Pure Appl. Chem. 70, 985-991.
9. Bernauer, K., Ghizdavu, S. & Verardo, L. 1999 Chiral metal complexes as probes in electron-transfer reactions involving metalloproteins. Coord. Chem. Rev. 190-192, 357-369.
10. Boswell, A. P., Eley, C. G. S., Moore, G. R., Robinson, M. N., Williams, G., Williams, R. J. P., Neupert, W. J. & Hennig, B. 1982 Proton NMR studies of eukaryotic cytochrome c. Resonance assignments and iron-hexacyanide-mediated electron exchange. Eur. J. Biochem. 124, 289-294.
11. Brautigan, D. L., Ferguson-Miller, S., Tarr, G. E. & Margoliash, E. 1978 Definition of cytochrome c binding domains by chemical modification. J. Biol. Chem. 253, 140-148.
12. Butler, K. J., Davies, D. M., Sykes, A. G., Koppenol, W. H., Osheroff, N. & Margoliash, E. 1981 Use of singly modified cytochrome c derivatives to determine the site for electron transfer in reactions with inorganic complexes. J. Am. Chem. Soc. 103, 469-471.
13. Butler, J., Chapman, S. K., Davies, D. M., Sykes, A. G., Speck, S. H., Osheroff, N. & Margoliash, E. 1983 Preferred sites for electron transfer between cytochrome c and iron and cobalt complexes. J. Biol. Chem. 258, 6400-6404.
14. Drake, P. L., Hartshorn, R. T., McGinnis, J. & Sykes, A. G. 1989 pH dependence of rate constants for reactions of cytochrome c with inorganic redox partners and mechanistic implications. Inorg. Chem. 28, 1361-1366.
15. -. FEBS Lett. 150, 293-299.
16. 3-. Inorg. Chem. 30, 4282-4285.
17. Isied, S. S., Worosila, G. & Atherton, S. J. 1982 Electron transfer across polypeptides. 4. Intramolecular electron transfer from ruthenium(II) to iron(III) in histidine-33 modified horse heart cytochrome c. J. Am. Chem. Soc. 104, 7659-7661.
18. 1 on cytochrome c. FEBS Lett. 111, 395-398.
19. Koppenol, W. H. & Margoliash, E. 1982 The asymmetric distribution of charges on the surface of horse cytochrome c. J. Biol. Chem 257, 4426-4437.
20. Moore, G. R., Eley, C. G. S. & Williams, G. 1984 Electron transfer reactions of class I cytochromes c. Advances in inorganic and bioinorganic mechanisms (ed. A. G. Sykes), vol. 3, pp. 1-96. London: Academic Press.
21. III in ruthenium-modified cytochrome c. J. Am. Chem. Soc. 106, 5145-5150.
22. Pettigrew, G. W. & Moore, G. R. 1987 Cytochromes c, biological aspects. Berlin: Springer.
23. Pettigrew, G. W. & Moore, G. R. 1990 Cytochromes c, evolutionary, structural and physicochemical aspects. Berlin: Springer.
24. 2-. Inorg. Chim. Acta 225, 151-156.
25. Sasaki, S., Nishijima, Y., Koga, H. & Ohkubo, K. 1989 Stereoselective electron-transfer reaction between ferrocytochrome c and tris(acetylacetonato) cobalt(III). Inorg. Chem. 28, 4061-4063.
26. Sasaki, S., Nishijima, Y., Koga, H. & Ohkubo, K. 1991 Chiral recognition of ferrocytochrome c(II) in electron-transfer reactions with cobalt(III) complexes. J. Chem. Soc. Dalton Trans. 1143-1148.
27. Sun, J., Su, C. & Wishart, J. F. 1996 Intramolecular electron transfer in pentaammineruthenium(III)-modified cobaltocytochrome c. Inorg. Chem. 35, 5893-5901.
28. Webb, M., Stonehuerner, J. & Millett, F. 1980 The use of specific lysine modifications to locate the reaction site of cytochrome c with sulfite oxidase. Biochim. Biophys. Acta Bio-energetics 593, 290-298.
29. Williams, G., Eley, C. G. S., Moore, G. R. & Williams, R. J. P. 1982 Proton NMR studies of the electron exchange between cytochrome c and iron hexacyanides. Definition of the iron hexacyanide binding sites on cytochrome c. Eur. J. Biochem. 124, 295-303.
30. Winkler, J. R., Nocera, D. G., Yocom, K. M., Bordignon, E. & Gray, H. B. 1982 Electron-transfer kinetics of pentaammineruthenium (III)(histidine-33)- ferricytochrome c. Measurement of the rate of intramolecular electron transfer between redox centres separated by 15 Å in a protein. J. Am. Chem. Soc. 104, 5798-5800.
31. Yocom, K. M., Shelton, J. B., Shelton, J. R., Schroeder, W. A., Worosila, G. W., Isied, S. S., Bordignon, E. & Gray, H. B. 1982 Preparation and characterization of a pentaammine-ruthenium(III) derivative of horse heart ferricytochrome c. Proc. Natl Acad. Sci. USA 79, 7052-7055.