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Redox Reactions of Bio Molecule for Nano-bio Battery

Published online by Cambridge University Press:  01 February 2011

Kwang Min Shin
Affiliation:
coolskm@ihanyang.ac.krHanyang UniversitySeoul N/A N/AKorea, Republic of
Sang Jun Park
Affiliation:
sjpark92@ihanyang.ac.kr, Hanyang University, Seoul, N/A, N/A, Korea, Republic of
Seong Gil Yoon
Affiliation:
pandasky@ihanyang.ac.kr, Hanyang University, Seoul, N/A, N/A, Korea, Republic of
Chang Kee Lee
Affiliation:
withs@ihanyang.ac.kr, Hanyang University, Seoul, N/A, N/A, Korea, Republic of
Su Ryon Shin
Affiliation:
srshin@ihanyang.ac.kr, Hanyang University, Seoul, N/A, N/A, Korea, Republic of
Min Kyoon Shin
Affiliation:
masscsq@ihanyang.ac.kr, Hanyang University, Seoul, N/A, N/A, Korea, Republic of
Bon Kang Gu
Affiliation:
bons1020@ihanyang.ac.kr, Hanyang University, Seoul, N/A, N/A, Korea, Republic of
Min Sup Kim
Affiliation:
kimins21@ihanyang.ac.kr, Hanyang University, Seoul, N/A, N/A, Korea, Republic of
Seon Jeong Kim
Affiliation:
sjk@hanyang.ac.kr, Hanyang University, Seoul, N/A, N/A, Korea, Republic of
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Abstract

Metal oxide nanoparticles within the protein ferritin can act as an energy storage source in nano-bio batteries containing ferrous ferritin and a reconstituted ferritin cage containing different inorganic elements, such as Co, Mn, Ni, and Pt. These components were introduced as two ferritin half-cells with different redox potentials existing between the ferrous ferritin and the reconstituted ferritin. The reduction of ferritin was analyzed in a solution containing 3-[N-morpholino] propanesulfonic acid buffer and oxidized methyl viologen using cyclic voltammetry. The reduction and oxidation peaks of the methyl viologen occurred at potentials of −300 and −100 mV, respectively, and the reduction and the oxidation peaks of the released Fe occurred at potentials of −300 and −100 mV, respectively. The reduction of ferritin was influenced by the pH of the ferritin solution.

Type
Research Article
Copyright
Copyright © Materials Research Society 2006

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References

1 Chu, S.H., Choi, S.H., Watt, G.D., Kim, J.W., Park, Y., Davis, R.C., Harb, J.N., King, G.C., Lillehei, P.H., The International Society for Optical Engineering, Proceedings of SPIE's Smart structure and Materials, edited by Varadan, V.K., (vol. 5389, 2004) pp 443452.Google Scholar
2 Kim, J.W., Choi, S.H., Lillehei, P.H., King, G.C., Elliott, J.R., Chu, S.H., Park, Y., Watt, G.D., Electrochemical Society, 206th Meeting of the Elec. Soc. (vol. 6, 2004) pp 547562.Google Scholar
3 King, G.C., Choi, S.H., Chu, S.H., Kim, J.W., Park, Y.J., Lillehei, P., Watt, G.D., Davis, R., Harb, J.N., The International Society for Optical Engineering, Proceedings of SPIE’s Smart structure and Materials edited by Varadan, V.K., (vol. 5389, 2004) pp 462468.Google Scholar
4 Harrison, P.M. and Arosio, P., Biochim. Biophys. Acta, 1275, 161 (1996).Google Scholar
5 Watt, G.D., Frankel, R.B., and Papaefthymiou, G.C., Proc. of the Natl. Acad. of Sci. of U.S.A., (vol. 82, 1985) pp 36403643.Google Scholar
6 Douglas, T., and Stark, V.T., Inor. Chem., 39, 1828 (2000).Google Scholar
7 Meldrum, F.C., Wade, V.J., Nimmo, D.L., Heywood, B.R., and Mann, S., Nature, 349, 684 (1991).Google Scholar
8 Corbin, J.L., Watt, G.D.., Analytical Biochem., 186, 86 (1990).Google Scholar
9 Treffry, A., Harrison, P.M., Biochem. J., 171, 313 (1978).Google Scholar
10 Martin, T.D., Monheit, S.A., Niichel, R.J., Peterson, S.C., Campbell, C.H., and Zapien, D.C., J. Elect. Chem., 420, 279 (1997).Google Scholar