Coupling to lysine-13 promotes electron tunneling through carboxylate-terminated alkanethiol self-assembled monolayers to cytochrome c

Journal of Physical Chemistry B

Volumn 107, Issue 37, 2003, Pages 9947-9949

  Niki, Katsumi ^a,b   Hardy, W Reef ^b   Hill, Michael G ^b   Li, H ^c   Sprinkle, James R ^d   Margoliash, Emanuel ^c,e   Fujita, Kyoko ^a,f   Tanimura, Ryutaro ^a,f   Nakamura, Nobufumi ^f   Ohno, Hiroyuki ^f   Richards, John H ^a   Gray, Harry B ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^b OCCIDENTAL COLLEGE   (United States)

^c UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^d NORTHEASTERN ILLINOIS UNIVERSITY   (United States)

^e NORTHWESTERN UNIVERSITY   (United States)

^f TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLATION; ELECTROCHEMISTRY; ELECTRON TRANSPORT PROPERTIES; ELECTRON TUNNELING; ELECTRONIC STRUCTURE; INTERFACES (MATERIALS); PROTEINS; SELF ASSEMBLY; SUBSTITUTION REACTIONS; SURFACE TREATMENT;

ALANINE; ALKANETHIOL SELF ASSEMBLED MONOLAYERS; ARGININE; CYTOCHROME; LYSINE;

MONOLAYERS;

EID: 0141570947     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp035392l     Document Type: Letter

References (30)

1. Theodorakis, J. L.; Armes, L. G.; Margoliash E. Biochim. Biophys. Acta 1995, 1252, 114-125 and references therein.
2. Bosshard, H. R. In Cytochrome c. A Multidisciplinary Approach; Scott, R. A., Mauk, A. G., Eds.; University Science Books: Sausalito, CA, 1996; pp 373-396.
3. Northrup, S. H.; Thomasson, K. A.; Miller C. M.; Barker, P. D.; Eltis, L. D.; Guillemette, J. G.; Inglis, S. C.; Mauk, A. G. Biochemistry 1993, 32, 6613-6623.
4. Döpner, S.; Hildebrandt, P.; Rosell, F. I.; Mauk, A. G.; von Walter, M.; Buse, G.; Soulimane, T. Eur. J. Biochem. 1999, 261, 379-391.
5. McLendon, G. Acc. Chem. Res. 1988, 21, 160-167.
6. Nocek, J. M.; Zhou, J. S.; DeForest, S.; Priyadarshy, S.; Beratan, D. N.; Onuchic, J. N.; Hoffman, B. M. Chem. Rev. 1996, 96, 2459-2489.
7. (a) Zhen, Y.-J.; Hoganson, C.; Babcock, G. T.; Ferguson-Miller, S. J. Biol. Chem. 1999, 274, 38032-38041.
8. (b) Wang, K.; Zhen, Y.-J.; Sadoski, R.; Grinnell, S.; Geren, L.; Ferguson-Miller, S.; Durham, B.; Millett, F. J. Biol. Chem. 1999, 274, 38042-38050.
9. Flöck, D.; Helms, V. Proteins 2002, 47, 75-85.
10. Leesch, V. W.; Bujons, J.; Mauk, A. G.; Hoffman, B. M. Biochemistry 2000, 39, 10132-10139.
11. Beratan, D. N.; Betts, J. N.; Onuchic, J. N. Science 1991, 252, 1285-1288.
12. (a) Wuttke, D. S.; Bjerrum, M. J.; Winkler, J. R.; Gray, H. B. Science 1992, 256, 1007-1009.
13. (b) Langen, R.; Chang, I.-Jy.; Germanas, J. P.; Richards, J. H.; Winkler, J. R.; Gray, H. B. Science 1995, 268, 1733-1735.
14. (c) Gray, H. B.; Winkler, J. R. Annu. Rev. Biochem. 1996, 65, 537-561.
15. Tarlov, M. J.; Bowden, E. F. J. Am. Chem. Soc. 1991, 113, 1847-1849.
16. Collinson, M.; Bowden, E. F.; Tarlov, M. J. Langmuir 1992, 8, 1247-1250.
17. Song, S.; Clark, R. A.; Bowden, E. F.; Tarlov, M. J. J. Phys. Chem. 1993, 97, 6564-6572.
18. Kasmi, A. E.; Wallace, J. M.; Bowden, E. F.; Binet, S. M.; Linderman, R. J. J. Am. Chem. Soc. 1998, 120, 225-226.
19. Feng, Z. Q.; Imabayashi, S.; Kakiuchi, T.; Niki, K. J. Electroanal. Chem. 1995, 394, 149-154.
20. Arnold, S.; Feng, Z. Q.; Kakiuchi, T.; Knoll, W.; Niki, K. J. Electroanal. Chem. 1997, 438, 91-97.
21. Feng, Z. Q.; Imabayashi, S.; Kakiuchi, T.; Niki, K. J. Chem. Soc., Faraday Trans. 1997, 93, 1367-1370.
22. Avila, A.; Gregory, B. W.; Niki, K.; Cotton, T. M. J. Phys. Chem. B 2000, 104, 2759-2766.
23. Niki, K. Electrochemistry 2002, 70, 82-90.
24. Andrew, S. M.; Thomasson, K. A.; Northrup S. H. J. Am. Chem. Soc. 1993, 115, 5516-5521.
25. Niki, K.; Sprinkle, J. R.; Margoliash, E. Bioelectrochemistry 2002, 55, 37-40.
26. Niki, K.; Pressler, K. R.; Sprinkle, J. R.; Li, H.; Margoliash, E. Russ. J. Electrochem. 2002, 38, 74-78.
27. Tanimura, R.; Hill, M. G.; Margoliash, E.; Niki, K.; Gray, H. B. Electrochem. Solid-State Lett. 2002, 5, E67-70.
28. Laviron, E. J. Electroanal. Chem. 1979, 101, 19-28.
29. -1.
30. Yeast iso-1 cyt c (C102S) has an arginine at position 13. The mutant RC9-K13R was therefore prepared and investigated electrochemically. Mutant ET rates through HOOC-SAMs are more than 100 times smaller than those of RC9 and are nearly identical with those of native yeast iso- 1 cyt c (Figure 3). These results implicate position 13 as the probable ET coupling site for both RC9-K13R and yeast iso-1 cyt c, although a lysine residue at position 11 in yeast iso-1 cyt c also could be involved.