• Title/Summary/Keyword: heme

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Heme과 Hemoglobin을 이용한 Pentachlorophenol 오염토양 정화

  • 강구영;정남현
    • Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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    • 2002.04a
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    • pp.49-53
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    • 2002
  • 워싱턴주 벤쿠버시 Bonneville 전력소 전주 보관 지역내 PCP와 creosote 오염토양 2g 당 0.020g heme에 0.108g $H_2O$$_2$을 혼합한 산화방법과 0.035g hemoglobin에 0.324g $H_2O$$_2$을 혼합한 산화방법을 비교ㆍ조사하였다. 오염토양에 $^{14}$ C-PCP을 첨가한 다음에 $^{14}$ C의 물질수지를 조사한 결과, 24시간동안 반응 후 $^{14}$ $CO_2$는 heme 과 hemoglobin반응에서는 각각 3.50g와 3.88% 생산되었다. $^{14}$ C 물질수지 분포는 heme 촉매 산화반응에서 용매 상에 43.01% 토양 상에는 46.03%이고, hemoglobin 촉매 산화반응에서는 용매 상에 39.21%와 토양 상에 51.25%로 비슷한 분포를 보였다. 실험실 규모 pan 실험에서 초기 PCP농도 273$\pm$20 mg/kg과 TPH 6379$\pm$45 mg/kg인 오염토양에서 hemoglobin 촉매 산화 반응이 초기반응을 제외하고 7일 이후 반응에서 heme 촉매 산화반응보다 빠르게 분해되었고, 35일 반응 이후 PCP는 10 mg/kg 이하의 값을 나타내었고, TPH도 유사한 결과를 보여 주었다. 그러므로 건조 hemoglobin과 과산화수소에 의한 PCP 오염토양 복원기술은 분해율이 높고 경제성을 가지고 있으므로 기존의 복원공정을 대안으로 제시될 수 있다.

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Theoretical Study on The Interaction Between Benzo(a)pyrene and Cytochrome P-450 (Benzo(a)pyrene 과 Cytochrome P-450의 대한 상호작용에 대한 이론적 연구)

  • 도성탁
    • Biomedical Science Letters
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    • v.1 no.1
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    • pp.89-94
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    • 1995
  • Considering the planar structure and nonpolar properity of benzo(a)pyrene(B(a)p) and the planar heme part of cytochrome P-450, stacking interaction is probable. MO calculation on B(a)P and heme part of cytochrome P-450 were carried out to dertermine probable stacking interaction models. In this case, orbital interaction is most important. Accordingly, the stacking positions have high eigen vector in frontier orbital and boning type between two molecules. In this way, five probate models were selected and examined by MN2 and MO method. The most probable .stacking interaction model which is the 4, 5, 6 positions of B(a)P overlap carbon atom and pyrrole ring of ring of heme group was determined.

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Bioavailability of Aspartic Acid Chelated Iron on Iron-deficient Rats (아스파르트산 킬레이트 철분의 철분 결핍쥐에서의 생물학적 유용성)

  • Park, Myoung-Gyu;Ha, Tae-Yul;Shin, Kwang-Soon
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.40 no.12
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    • pp.1720-1725
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    • 2011
  • Aspartic acid chelated iron (Asp-Fe) was synthesized by a new method using calcium carbonate, aspartic acid, and ferrous sulfate. This study was carried out to investigate the bioavailability of Asp-Fe in iron-deficient rats. We divided the rats into four experimental groups. The first was the normal diet control group, or NC. The second was the no treated control group of iron-deficient (ID) rats, or ID+C. The third was the heme-iron (heme-Fe) treated group of ID rats, ID+heme-Fe. And the fourth was the Asp-Fe treated group of ID rats, or ID+Asp-Fe. There were no differences among any of the experimental groups in diet consumption, change of body weight, or the weight of the livers, kidneys, or spleens. After 7 days of feeding, the iron content in the sera of the ID+Asp-Fe group (175.2 ${\mu}g$/dL) and the ID+heme-Fe group (140.8 ${\mu}g$/dL) were significantly higher than that of the ID-C group (96.1 ${\mu}g$/dL). The total iron binding capacity (TIBC) of the ID+Asp-Fe group (735.4 ${\mu}g$/dL) was significantly normalized compared to the ID+C group (841.9 ${\mu}g$/dL) or ID+heme-Fe group (824.6 ${\mu}g$/dL). The hematocrit level of the ID+Asp-Fe group was increased to normal levels, but there was no statistical difference among ID groups. The absorption ratio of heme-Fe was 21.3% and that of Asp-Fe was 50.2%, which indicates a 2.3 times higher ratio in comparison with heme iron. With the above results we found that Asp-Fe seems to be an efficient form of iron to supply iron deficient rats in order to cure them of anemia. Thus, these findings suggest that aspartic acid chelated iron has the potential to serve as a functional food related to iron metabolism.

Porphyrin Derivatives from a Recombinant Escherichia coli Grown on Chemically Defined Medium

  • Lee, Min Ju;Chun, Se-Jin;Kim, Hye-Jung;Kwon, An Sung;Jun, Soo Youn;Kang, Sang Hyeon;Kim, Pil
    • Journal of Microbiology and Biotechnology
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    • v.22 no.12
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    • pp.1653-1658
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    • 2012
  • We have reported previously that a recombinant Escherichia coli co-expresses aminolevulinic acid (ALA) synthase, an NADP-dependent malic enzyme, and a dicarboxylate transporter-produced heme, an iron-chelated porphyrin, in a succinate-containing complex medium. To develop an industrially plausible process, a chemically defined medium was formulated based on M9 minimal medium. Heme synthesis was enhanced by adding sodium bicarbonate, which strengthened the C4 metabolism required for the precursor metabolite, although a pH change discouraged cell growth. Increasing the medium pH buffering capacity (100mM phosphate buffer) and adding sodium bicarbonate enabled the recombinant E. coli to produce heme at rates 60% greater than those in M9 minimal medium. Adding growth factors (1 mg/l thiamin, 0.01 mg/l biotin, 5 mg/l nicotinic acid, 1 mg/l pantothenic acid, and 1.4 mg/l cobalamin) also induced positive heme production effects at levels twice of heme production in M9-based medium. Porphyrin derivatives and heme were found in the chemically defined medium, and their presence was confirmed by liquid chromatography/mass spectroscopy (LC/MS). The formulated medium allowed for the production of $0.6{\mu}M$ heme, $29{\mu}M$ ALA, $0.07{\mu}M$ coproporphyrin I, $0.21{\mu}M$ coproporphyrin III, and $0.23{\mu}M$ uroporphyrin in a 3 L pH-controlled culture.

Possible Role of Heme Oxygenase-1 and Prostaglandins in the Pathogenesis of Cerebral Malaria: Heme Oxygenase-1 Induction by Prostaglandin $D_2$ and Metabolite by a Human Astrocyte Cell Line

  • Kuesap, Jiraporn;Na-Bangchang, Kesara
    • Parasites, Hosts and Diseases
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    • v.48 no.1
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    • pp.15-21
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    • 2010
  • Astrocytes are the most abundant cells in the central nervous system that play roles in maintaining the blood-brain-barrier and in neural injury, including cerebral malaria, a severe complication of Plasmodium falciparum infection. Prostaglandin (PG) $D_2$ is abundantly produced in the brain and regulates the sleep response. Moreover, $PGD_2$ is a potential factor derived from P. falciparum within erythrocytes. Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites. Here, we showed that treatment of a human astrocyte cell line, CCF-STTG1, with $PGD_2$ significantly increased the expression levels of HO-1 mRNA by RT-PCR. Western blot analysis showed that $PGD_2$ treatment increased the level of HO-1 protein, in a dose- and time-dependent manner. Thus, $PGD_2$ may be involved in the pathogenesis of cerebral malaria by inducing HO-1 expression in malaria patients.

Effect of Gene Amplifications in Porphyrin Pathway on Heme Biosynthesis in a Recombinant Escherichia coli

  • Lee, Min Ju;Kim, Hye-Jung;Lee, Joo-Young;Kwon, An Sung;Jun, Soo Youn;Kang, Sang Hyeon;Kim, Pil
    • Journal of Microbiology and Biotechnology
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    • v.23 no.5
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    • pp.668-673
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    • 2013
  • A recombinant E. coli co-expressing ALA synthase (hemA), NADP-dependent malic enzyme (maeB), and dicarboxylic acid transporter (dctA) was reported to synthesize porphyrin derivatives including iron-containing heme. To enhance the synthesis of bacterial heme, five genes of the porphyrin biosynthetic pathway [pantothenate kinase (coaA), ALA dehydratase (hemB), 1-hydroxymethylbilane synthase (hemC), uroporphyrinogen III synthase (hemD), and uroporphyrinogen III decarboxylase (hemE)] were amplified in the recombinant E. coli co-expressing hemA-maeB-dctA. Pantothenate kinase expression enabled the recombinant E. coli to accumulate intracellular CoA. Intracellular ALA was the most enhanced by uroporphyrinogen III synthase expression, porphobilinogen was the most enhanced by ALA dehydratase expression, uroporphyrin and coproporphyrin were the most enhanced by 1-hydroxymethylbilane synthase expression. The strain co-expressing coaA, hemA, maeB, and dctA produced heme of $0.49{\mu}mol/g$-DCW, which was twice as much from the strain without coaA expression. Further pathway gene amplifications for the porphyrin derivatives are discussed based on the results.

14N Mines Pulsed-ENDOR of Proximal Histidine and Heme of Aquometmyoglobin and Fluormetmyoglobin

  • Lee, Hong-In
    • 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.

Dynamics of CO Rebinding to Protoheme in Viscous Solutions

  • Lee, Tae-Gon;Park, Jae-Heung;Kim, Joo-Young;Joo, Sang-Woo;Lim, Man-Ho
    • Bulletin of the Korean Chemical Society
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    • v.30 no.1
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    • pp.177-182
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    • 2009
  • We present the geminate rebinding kinetics measurements of CO to 2-methylimidazole (2-MeIm) bound ferrous protoporphyrin- IX (FePPIX) in alkaline glycerol/water mixtures at 293 K after photolysis. The kinetics was probed by monitoring the CO stretching mode using femtosecond vibrational spectroscopy. When 2-MeIm is used in excess, heme dimers that typically form in low viscosity solutions disappear as the viscosity of the solvent increases. Heme aggregates formed in low viscosity solutions turn monomeric as more 2-MeIm is added, suggesting that 6-coordinated heme, including a strong proximal histidine tends to be in the monomeric form. The vibrational band of CO in the 2-MeIM-FePPIX-CO is well described by a single Gaussian function centered at 1958 $cm^-1$ and 28 $cm^-1$ full width at half maximum. The efficiency and rate of the geminate rebinding of CO to the heme increase with viscosity of the solvent, suggesting that retention of the dissociated CO near the heme, for a longer period by the viscous solvent media, accelerates rebinding.

Effect of Heme Oxygenase Induction by NO Donor on the Aortic Contractility

  • Kim, Chang-Kyun;Sohn, Uy-Dong;Lee, Seok-Yong
    • The Korean Journal of Physiology and Pharmacology
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    • v.5 no.1
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    • pp.87-92
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    • 2001
  • Carbon monoxide (CO) binds to soluble guanylate cyclase to lead its activation and elicits smooth muscle relaxation. The vascular tissues have a high capacity to produce CO, since heme oxygenase-2 (HO-2) is constitutively expressed in endothelial and smooth muscle cells, and HO-1 can be greatly up-regulated by oxidative stress. Moreover, the substrate of HO, heme, is readily available for catalysis in vascular tissue. Although the activation of heme oxygenase pathway under various stress conditions may provide a defence mechanism in compromised tissues, the specific role of HO-1-derived CO in the control of aortic contractility still remains to be elucidated. The present study was done to determine the effect of HO-1 induction on the aortic contractility. Thus, the effects of incubation of aortic tissue with S-nitroso-N-acetylpenicillamine (SNAP) for 1 hr on the aortic contractile response to phenylephrine were studied. The preincubation with SNAP resulted in depression of the vasoconstrictor response to phenylephrine. This effect was restored by HO inhibitor or methylene blue but not by NOS inhibitor. The attenuation of vascular reactivity by preincubation with SNAP was also revealed in endothelium-free rings. $AlF4^--evoked$ contraction in control did not differ from that in SNP-treated group. These results suggest that increased production of CO was responsible for the reduction of the contractile response to phenylephrine in aortic ring preincubated with SNAP and this effect of SNAP was independent on endothelium.

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Assignment of the Redox Potentials of Cytochrome c₃of Desulfovibrio vulgaris Hildenborough by ¹H NMR

  • 박장수;강신원;신정휴
    • Bulletin of the Korean Chemical Society
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    • v.16 no.10
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    • pp.968-971
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    • 1995
  • The heme assignment of the 1H NMR spectrum of cytochrome c3 of Desulfovibrio vulgaris Hildenborough within the X-ray structure were fully cross established according to their redox potential. The major reduction of the heme turned out to take place in the order of hemes Ⅳ,Ⅰ,Ⅱ and Ⅲ(the heme numbers indicating the order of bonding to the primary sequence). This assignment can provide the physicochemical basis for the elucidation of electron transfer of this protein.