• Bulletin of the Korean Chemical Society
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• v.22 no.4
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• pp.413-416
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• 2001

• Journal of Nutrition and Health
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• v.30 no.10
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• pp.1188-1194
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• 1997

The aim of this was to investigate whether the regular consumption of kimchi influences the iron status (RBC , Hb, Ht, MCH, MCV, MCHC, transferrin , serum iron, and ferritin) in volunteers. Healthy male adults(n=12) took part in the study subdivided into the control Ⅰ-phase(for 2weeks), kimchi-phase (for 4 weeks), and control Ⅱ-phase(for 2 weeks). In addition to their normal diet, participant consumed 300g of lactic acid fermented Chinese cabbage kimchi daily for four weeks. In the control Ⅰ and control Ⅱ phases, the participants kept up their normal diets without consuming any fermented foods. Dietary intakes were recorded for 3 consecutive days in each phase, with the aid of household measures. Every two weeks. blood specimens were analysed. Significant differences(p<0.05) between the phases were found in MCHC, and transferrin in blood were not significantly changed during kimchi consumption. However, serum iron and ferritin levels were significantly increased(p<0.05) during kimchi consumption, achieving the highest levels in the fourth week of the kimchi components(ascrobic acid, sulfer compound, organic acid, capsaicin, gingerol , allicin). Because of lacticacid fermented kimchi's potential to prevent anemia , the consumption of this food can be recommended.

• Journal of Microbiology
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• v.39 no.3
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• pp.149-153
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• 2001

The electron transfer reaction is one of the most essential processes of life. Not only does it provide the means of transforming solar and chemical energy into a utilizable form for all living organisms, it also extends into a range of metabolic processes that support the life of a cell. Thus, it is of great interest to understand the physical basis of the rates and reduction potentials of these reactions. To identify the major determinants of reduction potentials in redox proteins, we have chosen the simplest electron transfer protein, rubredoxin, a small (52-54 residue) iron-sulfur protein family, widely distributed in bacteria and archaea. Rubredoxins can be grouped into two classes based on the correlation of their reduction potentials with the identity of residue 44; those with Ala44 (ex: Pyrococcus furiosus) have reduction potentials that are ∼50 mV higher than those with Va144 (ex: Clostridium pasteurianum). Based on the crystal structures of rubredoxins from C. pasteurianum and P. furiosus, we propose the identity of residue 44 alone determines the reduction potential by the orientation of the electric dipole moment of the peptide bond between 43 and 44. Based on 1.5 $\AA$ resolution crystal structures and molecular dynamics simulations of oxidized and reduced rubredoxins from C. pasteurianum, the structural rearrangements upon reduction suggest specific mechanisms by which electron transfer reactions of rubredoxin should be facilitated.