• Bulletin of the Korean Chemical Society
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• v.23 no.12
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• pp.1769-1772
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• 2002

Previous $^{19}F\;and\;^{1,2}H$ electron-nuclear double resonance (ENDOR) study of fluorometmyoglobin (MbF) in frozen-solution state provided sensitive tools sensing subtle structural changes of the heme that are not obtainable from X-ray. [Fann et al., J. Am. Chem. Soc. 1995, 117, 6019] Because of the intrinsic inhomogeneouse EPR line broadening effect of MbF in frozen-solution state, detection of the intrinsic inhomogeneouse EPR line broadening effect of MbF in frozen-solution state, detection of the electronic and geometrical changes of the heme ring itself and the proximal histidine by using $^{14}N$ CW ENDOR was interfered. In the present study, hyperfine-sensitive $^{14}N$ Mims ENDOR technique of pulsed-EPR was employed to probe the changes. With two different $\tau$ values of 128 and 196 ns, $^{14}N$ ENDOR signals of the heme and proximal histidine were completely resolved at $g'_{II}(=g_e=2)$. This study present that X-band $^{14}N$ Mims ENDOR sequence can sensitively detect the small changes of the spin densities and p orbital populations of the proximal and the heme nitrogens, caused by ligand and pH variation of the distal site.

• Journal of the Korean Magnetic Resonance Society
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• v.4 no.2
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• pp.91-102
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• 2000

The photoproduced cation radical of N-methylphenothiazine doped in the different kind of matrices of phenyltriethoxysilane (PhiTEOS), vinyltriethoxysilane (VTEOS), and methyloiethoxysilane (METOS) was comparatively studied with electron spin resonance (ESR) and electron nuclear double resonance (ENDOR). The photoinduced charge separation efficiency was determined by integration of ESR spectra which correspond to the amount of photoproduced cation radical in the matrices. This was correlatively studied with the polarity and pore size of the gel matrices. The polarity of the matrices was comparatively determined by measuring λ$\sub$max/ values of PC$_1$ in the different matrices. The relative pore size among the matrices was determined by measuring relative proton matrix ENDOR line widths of the photoproduced cation radical of PCI. The decay kinetic constants of the cation radical of PCI in the different matrices was relatively studied with fitting the biexponential decay curves after exposure into the ambient condition. This is correlatively interpreted with the polarity and pore size of the matrices.

• Journal of the Korean Magnetic Resonance Society
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• v.6 no.2
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• pp.103-112
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• 2002

The photoproduced cation radical of N-methylphenothiazine $(PC_1)$ doped into phenyltriehtoxysilane (PhiTEOS), vinyltriethoxysilane (VTEOS) and methyltriethoxysilane (METOS) was studied with electron spin resonance (ESR) and electron nuclear double resonance (ENDOR). The photoinduced charge separation efficiency was determined by integration of ESR spectra which correspond to the amount of photoproduced cation radical in the matrices. This was correlatively studied with the polarity and pore size of the gel matrices. The relative polarity of the matrices was determined by measuring ${\lambda}_{max}$ values of $PC_1$ in the different matrices. The relative pore size among the matrices was determined by measuring relative proton matrix ENDOR line widths of the photoproduced cation of $PC_1$. The decay kinetic constants of the cation radical of $PC_1$ in the different matrices with relatively studied with fitting the biexponential decay curves after exposure at the ambient condition. This is correlatively interpreted with the polarity and pore size of the matrices.

• Proceedings of the Korean Biophysical Society Conference
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• 2002.06b
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• pp.18-18
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• 2002

Nitrogenase, comprised of the MoFe and Fe proteins, catalyzes the reduction of dinitrogen to ammonia at ambient temperature and pressure. The MoFe protein contains two metal centers, the P-cluster (Fe8S7-8) and the FeMo-cofactor (Fe7S9：homocitrate), the substrate binding site. Despite the availability of the crystal structure of the MoFe protein, suprisingly little is known about the molecular details of catalysis at the active site, and no small-molecule substrate or inhibitor had ever been shown to directly interact with a protein-bound cluster of the functioning enzyme, until our electron-nuclear double resonance(ENDOR) study of CO-inhibited nitrogenase.(omitted)