Electron transfer from Zn-Protoporphyrin IX to ruthenium ammine attached at His63 of reconstituted cytochrome b562

Chemistry Letters

Volumn , Issue 7, 1999, Pages 551-552

  Hamachi, Itaru ^c   Takashima, Hiroshi ^c   Tsukiji, Shinya ^c   Shinkai, Seiji ^c   Nagamune, Teruyuki ^a   Oishi, Shigero ^b  

^a UNIVERSITY OF TOKYO   (Japan)

^b KITASATO UNIVERSITY   (Japan)

^c KYUSHU UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0033474678     PISSN: 03667022     EISSN: None     Source Type: Journal    
DOI: 10.1246/cl.1999.551     Document Type: Article

References (17)

1. a) A. Haniman and J. P. Sauvage, Chem. Soc. Rev., 1996, 41.
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6. For example, Zn-Cyt-c and Zn-Mb were reported; a) H. Elias, M. H. Chou, and J. R. Winkler, J. Am. Chem. Soc., 110, 429 (1988).
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11. MALDI-TOF mass mainly gave a molecular peak at 11881 corresponding to apo-protein plus ruthenium complex. Similar fragmentation during ionization was reported, see a) P. D. Barker, E. P. Nerou, S. M. V. Freund, and I. M. Fearnley, Biochemistry, 34, 15191 (1995).
12. b) C. W. Fenwick, A. M. English, and J. F. Wishart, J. Am. Chem. Soc., 119, 4758 (1997).
13. Digestion condition : enzyme / Cyt-b562 = 1/50 (w/w), 10 mM TrisHCl buffer, pH 8.0, 37 °C, 6 h. The digestion reaction was terminated by freezing the solution at -30 °C.
14. Sequences 1-15 (MW 1735), 96-104 (MW 1118 including 102-His), 33-42 (MW 1074), 86-95 (MW 1058) were detected. Other digested peptides couldn't be identified clearly in the TOF mass, because of their low MW.
15. The sample solution (10 μM, pH 8.0, 25 °C) was deaerated by argon bubbling for 30 min before measurement (N2-Dye (PLD457) laser).
16. This value is caluculated on the following equation: ket = 1/τl -1/τo.
17. M. J. Therien, B. E. Bowler, M. A. Selman, H. B. Gray, I. J. Chang, and J. R. Winkler, In ACS Advances in Chemistry Series; J. R. Bolton , N. Mataga, and G. McLendon, Eds.; American Chemical Society : Washington, DC, 228, 191(1991).