cytochrome-c-t has been researched along with phthalocyanine* in 2 studies
2 other study(ies) available for cytochrome-c-t and phthalocyanine
Article | Year |
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Synthesis of phthalocyanine stabilized rhodium nanoparticles and their application in biosensing of cytochrome c.
A single step synthesis route is described for the preparation of rhodium nanoparticles using a cobalt aminophthalocyanine macrocyclic complex as a stabilizer. The results of nanoparticles characterization using electronic absorption, Raman and X-ray spectroscopes as well as transmission electron microscopy are reported. Rhodium nanoparticle modified electrode behavior as examined by cyclic and differential pulse voltammetry is also provided. The nanoparticles were found to be well dispersed and stabilized throughout the macromolecular matrix. TEM studies showed that they have an average diameter of 3 to 5 nm with spherical shape. The colloidal rhodium was then used for electrochemical sensing of cytochrome c using glassy carbon electrode. The results showed that the colloidal rhodium nanoparticles enhanced the electron transfer process between cytochrome c and the electrode. Differential pulse voltammetric measurements of cytochrome c at the colloidal rhodium nanoparticles modified glassy carbon electrode showed a linear relationship with the oxidation peak currents in the concentration range of 100 nM to 3 microM of cytochrome c. Topics: Biosensing Techniques; Cytochromes c; Electrochemistry; Electrodes; Indoles; Isoindoles; Microscopy, Electron, Transmission; Nanoparticles; Oxidation-Reduction; Rhodium; Sensitivity and Specificity; Spectrum Analysis; X-Ray Diffraction | 2009 |
Radiation damage in biomimetic dye molecules for solar cells.
A significant obstacle to organic photovoltaics is radiation damage, either directly by photochemical reactions or indirectly via hot electrons. Such effects are investigated for biomimetic dye molecules for solar cells (phthalocyanines) and for a biological analog (the charge transfer protein cytochrome c). Both feature a central transition metal atom (or H(2)) surrounded by nitrogen atoms. Soft x-ray absorption spectroscopy and photoelectron spectroscopy are used to identify three types of radiation-induced changes in the electronic structure of these molecules. (1) The peptide bonds along the backbone of the protein are readily broken, while the nitrogen cage remains rather stable in phthalocyanines. This finding suggests minimizing peptide attachments to biologically inspired molecules for photovoltaic applications. (2) The metal atom in the protein changes its 3d electron configuration under irradiation. (3) The Fermi level E(F) shifts relative to the band gap in phthalocyanine films due to radiation-induced gap states. This effect has little influence on the optical absorption, but it changes the lineup between the energy levels of the absorbing dye and the acceptor/donor electrodes that collect the charge carriers in a solar cell. Topics: Cytochromes c; Electrons; Indoles; Isoindoles; Models, Molecular; Molecular Structure; Photoelectron Spectroscopy; Pigments, Biological; Radiation; Radiation-Sensitizing Agents; X-Ray Absorption Spectroscopy | 2009 |