• 한국지하수토양환경학회:학술대회논문집
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• 한국지하수토양환경학회 2002년도 총회 및 춘계학술발표회
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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.

• 대한의생명과학회지
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• 제1권1호
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• pp.89-94
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• 1995

B(a)P와 cytochrome P-450의 heme부분은 구조가 평면이므로 겹침 상호작용이 가능하다. 가능성이 큰 겹침 상호작용모형을 결정하기 위해 이들 분자에 대해 MO계산을 행하였다. 이 경우 궤도함수 상호작용이 가장 중요하므로, 프론티어궤도함수의 eigen vetor값이 크며 상호 결합성을 보여야 한다. 이를 바탕으로 다섯가지 가능성이 있는 모형을 선택한 수 MN2와 MO방법을 실행하였다. 이중 B(a)P의 4, 5, 6번 위치와 heme group의 Y탄소와 III pyrrole환이 포개어지는 형태가 가장 안전하였다.

• 한국식품영양과학회지
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• 제40권12호
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• pp.1720-1725
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• 2011

본 연구에서는 아스파르트산, 탄산칼슘 및 황산철을 반응시켜 아스파르트산 킬레이트 철분(aspartic acid chelated iron, Asp-Fe)을 제조하고 Asp-Fe의 철분결핍 쥐(iron-deficient rat, ID)에서의 생물학적 유용성을 확인하였다. 시험군은 철분이 함유된 식이를 섭취한 정상군(NC), 철분 결핍식이를 1개월간 투여하여 철분 결핍 상태를 유도한 쥐(ID)에 생리식염수를 공급한 결핍 대조군(ID+C), 철분 결핍 쥐에 햄철(heme-Fe) 투여군(ID+heme-Fe) 및 Asp-Fe 투여군(ID+Asp-Fe)으로 나누어 실시하였다. 그 결과 식이섭취량, 장기무게, 체중증가 정도에서 각 군에 따른 차이가 없는 것으로 나타났다. 7일간 투여 후 혈액 중 철분의 함량을 측정한 결과 결핍쥐에 Asp-Fe 투여군(175.2 ${\mu}g$/dL)과 heme-Fe 투여군(140.8 ${\mu}g$/dL)은 결핍 대조군(96.1 ${\mu}g$/dL)보다 유의적인 수준으로 증가하였다. 총 철분 결합능(total iron binding capacity, TIBC)를 측정한 결과 Asp-Fe 투여군(735.4 ${\mu}g$/dL)은 결핍 대조군(841.9 ${\mu}g$/dL)보다 유의적 수준으로 정상화되었다. 헤마토크리트(HCT) 수치를 측정한 결과에서 Asp-Fe 및 heme-Fe 모두 결핍 대조군보다 증가하는 경향은 보였지만 유의적인 차이는 없었다. 흡수율에서는 heme-Fe의 경우 21.3%인 반면에 Asp-Fe의 경우 50.2%로 약 2.3배 높은 것으로 나타났으며, 혈청에서의 철분농도 및 transferrin saturation(TS)는 heme-Fe 투여군 및 결핍 대조군에 비하여 Asp-Fe 투여군이 유의하게 높은 수준을 유지하였다. 이상의 결과로 미루어 볼 때 아미노산 킬레이트 철분은 heme-Fe과 유사한 수준의 생체 이용율을 가지고 있으며, 철분 결핍을 회복시키는데 매우 효과적인 보충제로서 이용될 수 있을 것으로 사료된다.

• Journal of Microbiology and Biotechnology
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• 제22권12호
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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.

• Parasites, Hosts and Diseases
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• 제48권1호
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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.

• Journal of Microbiology and Biotechnology
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• 제23권5호
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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.

• Bulletin of the Korean Chemical Society
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• 제23권12호
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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.

• Bulletin of the Korean Chemical Society
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• 제30권1호
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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.

• The Korean Journal of Physiology and Pharmacology
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• 제5권1호
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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.

• Bulletin of the Korean Chemical Society
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• 제16권10호
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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.