• Journal of the Korean Chemical Society
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• v.57 no.5
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• pp.560-567
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• 2013

A series of new Iron(II) Schiff base amino acid complexes derived from the condensation of amino acid and sodium 2-hydroxybenzaldehyde-5-sulfonate have been synthesized. The complexes were characterized by elemental, electronic, IR spectral analyses and conductance measurements. The stability and solubility of the prepared complexes were determined. Two spectral methods used to determine the stoichiometry of the prepared complexes which exhibited divalent tridentate coordination and formed chelates of octahedral structures. The antibacterial activity of the prepared complexes has been tested against Bacillus cereus, Pseudomonas aeruginosa and Micrococcus bacteria. The effect of HCl on investigated complexes studied spectrophotometrically.

• Asian-Australasian Journal of Animal Sciences
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• v.18 no.10
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• pp.1485-1491
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• 2005

This experiment was conducted to investigate the effects of iron from an amino acid complex (Availa-$Fe^{\circledR}$) on the iron status of neonatal and suckling piglets. A total of 24 gestating sows (Landrace${\times}$Large White) were randomly allocated to three dietary treatments. The control diet contained 80 mg $kg^{-1}$ Fe from ferrous sulfate heptahydrate ($FeSO_4$.$7H_2O$), while the two experimental diets were supplemented with an additional 120 mg $kg^{-1}$ Fe from Availa-$Fe^{(R)}$ or $FeSO_4$.$7H_2O$, respectively. The lactating sows remained the same iron treatments as gestating sows, while neonatal piglets of 24 litters born from the above sows were allotted to another three treatments. Piglets from the sows of the control treatment were fed basal diet with no supplemental Fe as control treatment, but were injected with 100 mg Fe as Fe dextran at birth. Piglets from the sows of Availa-$Fe^{(R)}$ or $FeSO_4$.$7H_2O$ treatments were supplemented with 120 mg $kg^{-1}$ iron from Availa-$Fe^{(R)}$ or $FeSO_4$.$7H_2O$, respectively. The total born alive and weaned, and the average piglets weight at birth and at weaning were not significantly affected by the sow' dietary treatments (p>0.05). Iron from Availa-$Fe^{(R)}$ did not demonstrate a statistically significant improvement in hemoglobin concentration, hematocrit and plasma iron of sows on day 90 and 105 of pregnancy and the milk iron of sows during lactation (p>0.05). Neonatal piglets in the Availa-$Fe^{(R)}$ treatment had a significantly higher hemoglobin concentration (p<0.05) and higher hematocrit and plasma iron (p>0.05) than those in the other two treatments, respectively. The hemoglobin of suckling piglets in the Availa-$Fe^{(R)}$ treatment was higher than that of piglets in $FeSO_4$.$7H_2O$ treatment on day 28 (p<0.05). The total iron binding capacity of piglets in Availa-$Fe^{(R)}$ treatment was lower than that of piglets in the control and $FeSO_4$.$7H_2O$ treatment on day 14 (p<0.05), but there was not a statistically significant difference among three treatments on day 28 (p>0.05). However, the hemoglobin and hematocrit of suckling piglets injected with Fe were higher than those of piglets in the other two treatments (p<0.05). This study indicated that the addition of 120 mg $kg^{-1}$ iron from amino acid complex into the diets improved iron status of neonatal and nursing piglets more effectively than the addition of 120 mg $kg^{-1}$ iron from $FeSO_4$.$7H_2O$, however, this improvement of the organic Fe was not sufficient to replace the Fe injection for prevention of iron-deficiency anemia.

• Textile Coloration and Finishing
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• v.25 no.4
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• pp.247-253
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• 2013

The enzyme-like catalytic functions of metal complex phthalocyanine derivatives those containing carboxylic acid groups could be applied as odor-removing systems and antibacterial systems. Pyromellitic dianhydride and 4-nitrophthalimide were used as starting material for synthesizing dinitro-tetracarboxylic acid iron phthalocyanine(compound 1). Then diamino-tetracarboxylic phthalocyanine(compound 2) was obtained by reduction of compound 1. For the formation of covalent bond with cellulose fiber, cyanuric chloride was introduced to the amino group of compound 2 by condensation reaction compound 3. The exhaustion method was employed for adsorbing compound 3 on cotton fiber. K/S values of each fabrics were measured by a CCM system and deodorizing rates were tested by a detector tube method for ammonia gas. K/S values of treated cotton fiber with compound 3 were arranged from 2.1 to 4.2 at $90^{\circ}C$ of exhaustion temperature. Deodorizing rates provided result of 81%, 84%, 88%, 91%, by passing time of 30 min, 60 min, 90 min, 120 min, respectively.

• Journal of Life Science
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• v.9 no.6
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• pp.743-752
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• 1999

The purpose of the paper is to explore the current knowledge on the nutritional evaluation, cholesterol-lowering effect and antitumor activity of kimchi and its ingredients(Korean cabbage, garlic, red pepper powder, ginger and onion). Kimchi contains high contents of nutrients such as vitamins(ascorbic acid, $\beta$-carotene and vitamin B complex), minerals(calcium, potassium, iron and phosphorous), essential amino acids and dietary fiber. Kimch also contains high levels of lactic acid bacteria, allicin, capsaicin, organic acid, phenol compounds, flavonoid and sulfur compounds. The dietary fiber and lactic acid bacteria isolated from kimchi are effective in improving intestinal microflora of human. Isoluble dietary fiber shows anticancer activity, but soluble dietary fiber shows hypocholesterolemic effect. Lactic acid bacteria isolated from kimchi acts as a hypocholesterolemic or anticancer agent. A major ingredient of kimchi is mainly cruciferous and allium family vegetables, which were also reported to prevent cancer and atherosclerosis. It is suggested that kimchi is important not only as one of the traditional fermented Korean food but also as therapeutic agent for carcinogenesis and hypercholesterolemic state.

• Animal Bioscience
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• v.36 no.3
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• pp.498-505
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• 2023

Objective: This study was conducted to determine the optimal dose of novel iron amino acid complexes (Fe-Lys-Glu) by measuring laying performance, egg quality, egg iron (Fe) concentrations, and blood biochemical parameters in laying hens. Methods: A total of 1,260 18-week-old healthy Beijing White laying hens were randomly divided into 7 groups with 12 replicates of 15 birds each. After a 2-wk acclimation to the basal diet, hens were fed diets supplemented with 0 (negative control, the analyzed innate iron content was 75.06 mg/kg), 15, 30, 45, 60, and 75 mg Fe/kg as Fe-Lys-Glu or 45 mg Fe/kg from FeSO₄ (positive control) for 24 wk. Results: Results showed that compared with the negative and positive control groups, dietary supplementation with 30 to 75 mg Fe/kg from Fe-Lys-Glu significantly (linear and quadratic, p<0.05) increased the laying rate (LR) and average daily egg weight (ADEW); hens administered 45 to 75 mg Fe/kg as Fe-Lys-Glu showed a remarkable (linear, p<0.05) decrease in feed conversion ratio. There were no significant differences among all groups in egg quality. The iron concentrations in egg yolk and serum were elevated by increasing Fe-Lys-Glu levels, and the highest iron content was found in 75 mg Fe/kg group. In addition, hens fed 45 mg Fe/kg from Fe-Lys-Glu had (linear and quadratic, p<0.05) higher yolk Fe contents than that with the same dosage of FeSO₄ supplementation. The red blood cell (RBC) count and hemoglobin content (linear and quadratic, p<0.05) increased obviously in the groups fed with 30 to 75 mg Fe/kg as Fe-Lys-Glu in comparison with the control group. Fe-Lys-Glu supplementation also (linear and quadratic, p<0.05) enhanced the activity of copper/zinc-superoxide dismutase (Cu/Zn-SOD) in serum, as a result, the serum malonaldehyde content (linear and quadratic, p<0.05) decreased in hens received 60 to 75 mg Fe/kg as Fe-Lys-Glu. Conclusion: Supplementation Fe-Lys-Glu in laying hens could substitute for FeSO₄ and the optimal additive levels of Fe-Lys-Glu are 45 mg Fe/kg in layers diets based on the quadratic regression analysis of LR, ADEW, RBC, and Cu/Zn-SOD.

• Korean Journal of Food Science and Technology
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• v.25 no.1
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• pp.46-51
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• 1993

The inactivating effect of iron(II)-ascorbate complex (Fe-Asc) on various phages was previously reported. This paper describes the molecular target in the phage virion attacked by Fe-Asc. The effect of Fe-Asc on protein was investigated with bovine serum albumin and the structural protein of phage J1. There were no differences in the SDS-polyacrylamide gel electrophoresis (patterns of these two proteins when either they were treated) with Fe-Asc or not. Also, there were no changes in the amino acid composition and ultraviolet spectrum of the proteins. The effects of Fe-Asc on DNA was investigated with pUC18 DNA, M13mpB DNA and ${\lambda}$ DNA as well as DNA from phage J1. Fe-Asc caused initially nicking of the subsequently form of pUC18 DNA to yield the open circular form and then subsequently the linear form. Strand breaks were also confirmed with M13mp8 DNA and ${\lambda}$ DNA as well as J1 DNA. The results indicate that the strand breaks in phage DNA could be responsible for the inactivation of phages by Fe-Asc.

• Bulletin of the Korean Chemical Society
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• v.19 no.6
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• pp.654-660
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• 1998

$[Fe^{II}Fe^{III}BPLMP(OAc)_2](BPh_4)_2$ (1), a new model for the reduced form of the purple acid phosphatases, has been synthesized by using a dinucleating ligand, 2,6-bis[((2-pyridylmethyl)(6-methyl-2-pyridylmethyl)amino) methyl]-4-methylphenol (HBPLMP). Complex I has been characterized by X-ray diffraction method as having (μ-phenoxo)bis(acetato)diiron core. Complex 1 was crystallized in the monoclinic space group C2/c with the following cell parameters: a=41.620(6) Å, b=14.020(3) Å, c=27.007(4) Å, β=90.60(2)°, and Z=8. The iron centers in the complex 1 are ordered as indicated by the difference in the Fe-O bond lengths which match well with typical $Fe^{III}-O\; and\; Fe^{II}-O$ bond lengths. Complex 1 has been studied by electronic spectral, NMR, EPR, SQUID, and electochemical methods. Complex 1 exhibits strong bands at 592 nm, 1380 nm in $CH_3CN$ (ε = 1.0 × 103 , 3.0 × 102). These are assigned to $phenolate-to-Fe^{III}$ and intervalence charge-transfer transitions, respectively. Its NMR spectrum exhibits sharp isotropically shifted resonances, which number half of those expected for a valence-trapped species, indicating that electron transfer between $Fe^{II}\;and\;Fe^{III}$ centers is faster than NMR time scale. This complex undergoes quasireversible one-electron redox processes. The $Fe^{III}_2/Fe^{II}Fe^{III}\;and\;Fe^{II}Fe^{III}/Fe^{II}_2$ redox couples are at 0.655 and -0.085 V vs SCE, respectively. It has $K_{comp}=3.3{\times}10^{12}$ representing that BPLMP/bis(acetate) ligand combination stabilizes a mixed-valence $Fe^{II}Fe^{III}$ complex in the air. Complex 1 exhibits a broad EPR signal centered near g=1.55 which is a characteristic feature of the antiferromagnetically coupled high-spin $Fe^{II}Fe^{III}$ system $(S_{total}=1/2)$. This is consistent with the magnetic susceptibility study showing the weak antiferromagnetic coupling $(J= - 4.6\;cm^{-1},\; H= - 2JS_1{\cdot}S2)$ between $Fe^{II}\; and \;Fe^{III}$center.

• Journal of Life Science
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• v.14 no.5
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• pp.752-760
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• 2004

The function of the [4Fe-4S] cluster containing iron (Fe-) protein in nitrogenase catalysis is to serve as the nucleotide-dependent electron donor to the MoFe protein which contains the sites for substrate binding and reduction. The ability of the Fe protein to function in this manner is dependent on its ability to adopt the appropriate conformation for productive interaction with the MoFe protein and on its ability to change redox potentials to provide the driving force required for electron transfer. The MgADP-bound (or off) conformational state of the nitrogenase Fe protein structure described reveals mechanisms for long-range communication from the nucleotide-binding sites to control affinity of association with the MoFe protein component. Two pathways, termed switches I and II, appear to be integral to this nucleotide signal transduction mechanism. In addition, the structure of the MgADP bound Fe protein provides the basis for the changes in the biophysical properties of the [4Fe-4S] observed when Fe protein binds nucleotides. The structures of the nitrogenase Fe protein with defined amino acid substitutions in the nucleotide dependent signal transduction pathways of the Switch I and Switch II have been determined by X-ray diffraction methods. These two pathways have been also implicated by site directed mutagenesis studies, structural analysis and analogies to other proteins that utilize similar nucleotide dependent signal transduction pathways. We have examined the validity of the assignment of these pathways in linking the signals generated by MgATP binding and hydrolysis to macromolecular complex formation and intermolecular electron transfer. The results provide a structural basis for the observed biophysical and biochemical properties of the Fe protein variants and interactions within the nitrogenase Fe protein-MoFe protein complex.

• Proceedings of the Korean Society of Crop Science Conference
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• 2017.06a
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• pp.36-36
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• 2017

Out of twenty common protein amino acids, there are many kinds of non protein amino acids (NPAAs) that exist as secondary metabolites and exert ecological functions in plants. Mimosine (Mim), one of those NPAAs derived from L. leucocephala acts as an iron chelator and reversely block mammalian cell cycle at G1/S phases. Cysteine (Cys) is decisive for protein and glutathione that acts as an indispensable sulfur grantor for methionine and many other sulfur-containing secondary products. Cys biosynthesis includes consecutive two steps using two enzymes-serine acetyl transferase (SAT) and O-acetylserine (thiol)lyase (OASTL) and appeared in plant cytosol, chloroplast, and mitochondria. In the first step, the acetylation of the ${\beta}$-hydroxyl of L-serine by acetyl-CoA in the existence of SAT and finally, OASTL triggers ${\alpha}$, ${\beta}$-elimination of acetate from OAS and bind $H_2S$ to catalyze the synthesis of Cys. Mimosine synthase, one of the isozymes of the OASTLs, is able to synthesize Mim with 3-hydroxy-4-pyridone (3H4P) instead of $H_2S$ for Cys in the last step. Thus, the aim of this study was to clone and characterize the cytosolic (Cy) OASTL gene from L. leucocephala, express the recombinant OASTL in Escherichia coli, purify it, do enzyme kinetic analysis, perform docking dynamics simulation analysis between the receptor and the ligands and compare its performance between Cys and Mim synthesis. Cy-OASTL was obtained through both directional degenerate primers corresponding to conserved amino acid region among plant Cys synthase family and the purified protein was 34.3KDa. After cleaving the GST-tag, Cy-OASTL was observed to form mimosine with 3H4P and OAS. The optimum Cys and Mim reaction pH and temperature were 7.5 and $40^{\circ}C$, and 8.0 and $35^{\circ}C$ respectively. Michaelis constant (Km) values of OAS from Cys were higher than the OAS from Mim. Inter fragment interaction energy (IFIE) of substrate OAS-Cy-OASTL complex model showed that Lys, Thr81, Thr77 and Gln150 demonstrated higher attraction force for Cys but 3H4P-mimosine synthase-OAS intermediate complex showed that Gly230, Tyr227, Ala231, Gly228 and Gly232 might provide higher attraction energy for the Mim. It may be concluded that Cy-OASTL demonstrates a dual role in biosynthesis both Cys and Mim and extending the knowledge on the biochemical regulatory mechanism of mimosine and cysteine.

• Journal of Life Science
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• v.26 no.6
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• pp.698-704
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• 2016

The intracellular transport of organelles and protein complexes is mediated by kinesin superfamily proteins (KIFs). The first kinesin, kinesin 1, was identified as a molecular motor protein that moves various organelles and protein complexes along the microtubule rails in cells. Kinesin 1 is a tetramer of two heavy chains (KHCs, also called KIF5s) and two kinesin light chains (KLCs). KIF5s interact with many different proteins through their tail region, but their binding proteins have not yet been fully identified. To identify the interaction proteins for KIF5A, we performed yeast two-hybrid screening and found a specific interaction with ferritin heavy chain (Frt-h), which has a role in iron storage and detoxification. Frt-h bound to the amino acid residues between 800 and 940 of KIF5A and to other KIF5s in the yeast two-hybrid assay. The coiled-coil domain of Frt-h is essential for interaction with KIF5A. In addition, ferritin light chain (Frt-l) interacted with KIF5s in the yeast two-hybrid assay. In addition, these proteins showed specific interactions in the glutathione S-transferase (GST) pull-down assay. An antibody to KHC specifically co-immunoprecipitated Frt-h and Frt-l from mouse brain extracts. These results suggest the kinesin 1 motor protein may transport the ferritin complex in cells.