1992 Fiscal Year Final Research Report Summary
Foundamental Studies on Bioelectric Devices
| Project/Area Number |
03044064
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| Research Category |
Grant-in-Aid for international Scientific Research
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| Allocation Type | Single-year Grants |
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| Section | Joint Research |
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| Research Institution | Yokohama National University |
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Principal Investigator |
NIKI Katsumi Yokohama National University, Professor, 工学部, 教授 (00017899)
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| Co-Investigator(Kenkyū-buntansha) |
GEORG TCHOMA アイオワ州立大学, 化学科, 博士研究員(助手)
THERESE M. C アイオワ州立大学, 化学科, 教授
HELMUT TRIBU ベルリン自由大学化学科ハーン. マイトナー研究所太陽エネルギー変換研究所, 所長, 教授
SAGARA Takamasa Yokohama National University, Instructor, 工学部, 助手 (20192594)
AKUTSU Hideo Yokohama National University, Professor, 工学部, 教授 (60029965)
TRIBUTSCH Helmut Berlin Free University, Germany, Professor (Hahn-Meitner Institu, Berlin)
COTTON Therese M. Iowa State University, U.S.A., Professor
TCHOMANOV Georg Iowa State University, U.S.A., Research Associate
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| Project Period (FY) |
1991 – 1992
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| Keywords | Bioelectoric device / cytochrome c / cytochrome C_3 / monolayer of electron-transfer protein / electron-transfer process / NMR / UV-vis reflectance spectroscopy / surface Raman scattering spectroscopy |
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| Research Abstract |
Cytochrome C_3, an electron-transfer possessing four hemes per molecule, is one of the most promising materials of the bioelectric devices due to its specific electrochemical and electric properties. The present study is devoted to the characterization of cytochrome C_3 solidstate film and of the monolayer of cytochrome immobilized on the electrode surface.
The Hall mobility of the cytochrome C_3 solid-state film was immeasurably small regardless of the oxidation state of cytochrome C_3. The resistivity of the film in its fully oxidized state was 10^<13> OMEGAcm.
The assignment of the NMR signals of hystidine and one phenylalanine residues was established. The study on the roles played by these residues on the intramolecular electrontransfer is now underway.
It was found from UV-vis reflectance spectroscopic measurement that (1) horse heart cytochrome c adsorbed on a bare surface maintains its native redox activity, which disappears after a short period, and (2) a thiol molecule possessing a carboxyl terminal group exhibits a function to regulate the redox potentials of cytochrome C_3.
Raman scattering signals of cytochrome c immobilized on the bis(4-pyridyl) disulfidemodified silver electrode could be selectively observed due to the resonance effect at a wavelength of the Soret band. The spin and coordination states of heme iron of cytochrome c were analyzed using Raman scattering techniques.
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