Abstract
Linear assemblies of cytochrome b 562 (cyt b 562) containing a chemically-modified heme molecule on the protein surface were constructed by successive intermolecular heme–heme pocket interactions and then immobilized onto a gold electrode via a heme molecule anchored on the electrode. The accumulation of the cyt b 562 units were confirmed by electrochemical analyses. The average number of proteins in each assembly was estimated to be about 6 units by quartz crystal microbalance and atomic force microscopy (AFM) analyses. The linear assemblies of the cyt b 562 units were clearly visualized by AFM as a rod-like architecture with a vertical orientation to the electrode surface.
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Acknowledgments
This work was supported by Grants-in-Aid for Scientific Research ((B) and Innovative Areas “Coordination Programming”, area 2107) from MEXT and the Japan Society for the Promotion of Science (JSPS). Y.K. acknowledges a support from the Global COE Program of Osaka University and from JSPS. A.O. acknowledges a support from the Frontier Research Base for Global Young Researchers, Osaka University, on the Program of MEXT, and from the Ogasawara Foundation. T.H. acknowledges a support from the Asahi Grass Foundation.
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This paper is dedicated to Prof. Dr. Hiroshi Nishihara for his outstanding contribution to the field of metal-containing polymers.
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Kakikura, Y., Onoda, A., Kubo, E. et al. Supramolecular Linear Assemblies of Cytochrome b 562 Immobilized on a Gold Electrode. J Inorg Organomet Polym 23, 172–179 (2013). https://doi.org/10.1007/s10904-012-9737-1
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DOI: https://doi.org/10.1007/s10904-012-9737-1