• Journal of the Korean Ceramic Society
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• v.53 no.5
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• pp.529-534
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• 2016

Nanocrystalline powder of zirconia stabilized with 8 mol% yttria (YSZ) has been synthesized through oxalate process using $ZrOCl_2{\cdot}8H_2O$ and $Y(NO_3)_3{\cdot}6H_2O$ as starting materials. Understanding of the characteristic changes of YSZ powder as a function of processing conditions is crucial in developing dense and porous microstructures required for fuel cell applications. In this research, microstructure change, surface area, particle shape and particle size were measured as a function of different processing conditions such as calcination temperature, stirring speed and concentration of starting materials. The resultant crystallite sizes were calculated by XRD-LB (X-Ray Diffraction Line-Broadening) method, BET method, and morphology of the crystal was observed in TEM and FE-SEM. The TEM examination showed that the powder synthesized with 0.7 M of YSZ concentration had a spherical morphology with sizes ranging from 20 to 40 nm. However, the powder was gradually aggregated above 1.0 M of YSZ concentration with the aggregation being intensified as the YSZ concentration was increased.

• BMB Reports
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• v.30 no.6
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• pp.397-402
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• 1997

A thiol-specific spin label was attached to cysteine-102 of yeast cytochrome c and electron paramagnetic resonance (EPR) spectra were measured as a function of added cytochrome c oxidase concentration. The intensity decreased due to line broadening as cytochrome c formed a complex with cytochrome c oxidase and reached a minimum when the ratio of cytochrome c to cytochrome c oxidase became one. Replacement of either Lys-72 or Lys-87 of cytochrome c by Glu did not result in a significant change in binding affinity. Interestingly the K72E mutant, unlike K87E, had a much lower rate of electron transfer than the wild type. These results indicate that many positively charged residues as a group participate in complex formation but Lys-72 might be important for cytochrome c to be locked in an orientation for an efficient electron transfer. A stoichiometry of 1 was also confirmed by optical absorption of the cytochrome c-cytochrome c oxidase complex which had been run through a gel chromatography cloumn to remove unbound cytochrome c. The EPR spectrum of this 1:1 complex, however, was a mixture of two components. This explains a biphasic kinetics for a single binding site on cytochrome c oxidase without invoking conformational transition.