• Journal of Microbiology and Biotechnology
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• 제13권5호
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• pp.647-650
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• 2003

In anhydrous organic solvents, the complexes formed between AOT (dodecylbenzene sulfuric acid sodium salt) and hemoproteins, such as hemoglobin, myoglobin, or cytochrome c, displayed remarkably higher activity than the hemoprotein powders to oxidize dibenzothiophene, a model compound of organic sulfurs contained in fossil fuels. In slightly hydrophobic organic solvents, such as ethyl acetate and butyl acetate, dibenzothiophene was completely oxidized catalytically by the cytochrome c-AOT complex with cumene hydroperoxide (${\alpha},{\alpha}-dimethylbenzyl$ hydroperoxide) as an oxidant. In highly hydrophobic organic solvents, such as decane and hexadecane, however, the activity of the cytochrome c-AOT complex decreased, presumably due to the aggregation of the hemoprotein-AOT complex in these solvents.

• 분석과학
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• 제8권2호
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• pp.117-124
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• 1995

지속적인 음주로 인하여 간경변증으로 사망한 human 간에서 ethanol에 의해서 유도되는 것으로 추측되는 hemoprotein들을 확인 및 부분정제하였다. 이 hemoprotein을 정제하기 위하여 Mohamed 등의 방법을 변형하여 단백질을 정제하였고, SDS-PAGE 및 spectrum 양상을 관찰하였다. Triton N-101을 처리한 crude extract를 준비하여 CO gas를 bubbling시킨 후 Octyl-Sepharose CL-4B column chromatography에서 0.06% Lubrol PX로 용출한 다음 0.25% Lubrol PX로 용출하였다(Fig. 2). 0.06% Lubrol PX로 용출한 active fraction을 Hydroxyapatite와 DEAE-Sephadex A-25 column으로 정제하였다(Fig. 3, 4). 정제한 단백질을 12.5% SDS-PAGE를 실시한 결과 분자량은 대조군으로 사용한 흰쥐 간에서 정제한 단백질의 분자량은 55 KDa와 52 KDa였고, 돌연사한 사람의 간에서 정제한 단백질의 분자량은 62 48KDa이며, 간경변증으로 사망한 사람의 간에서 정제한 단백질의 분자량은 54KDa였고(Fig. 5). Cytochrome P450 함량은 20.8nmol/mg protein이며 회수율은 약 4.1%이고, 이들의 최대흡수 파장은 446nm이었다(Fig. 6).

• Journal of Microbiology and Biotechnology
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• 제17권12호
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• pp.2066-2070
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• 2007

It was found that Shinorhizobium meliloti hemoprotein (SM) was more effective than Vitreoscilla hemoglobin (Vhb) in promoting secondary metabolites production when overexpressed in Streptomyces lividans TK24. The transformant with sm (sm-transformant) produced 2.7-times and 3-times larger amounts of actinorhodin than the vhb-transformant in solid culture and flask culture, respectively. In both solid and flask cultures, a larger amount of undecylprodigiocin was produced by the sm-transformant. It is considered that the overexpression of SM especially has activated the pentose phosphate pathway through oxidative stress, as evidenced by an increased NADPH production observed, and that it has promoted secondary metabolites biosynthesis.

• Biomolecules & Therapeutics
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• 제22권6호
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• pp.491-496
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• 2014

Photobiomodulation utilizes monochromatic (or quasimonochromatic) light in the electromagnetic region of 600~1000 nm for the treatment of soft tissues in a nondestructive and nonthermal mode. It is conceivable that photobiomodulation is based upon the ability of the light to alter cell metabolism as it is absorbed by general hemoproteins and cytochrome c oxidase (COX) in particular. Recently it has been suggested radiation of visible and infrared (IR) activates retrograde signaling pathway from mitochondria to nucleus. In this review, the role of COX in the photobiomodulation will be discussed. Further a possible role of water as a photoreceptor will be suggested.

• Journal of Microbiology and Biotechnology
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• 제33권12호
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• pp.1648-1656
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• 2023

We have previously observed that feeding with single-cell hemoprotein (heme-SCP) in dogs (1 g/day for 6 days) and broiler chickens (1 ppm for 32 days) increased the proportion of lactic acid bacteria in the gut while reducing their body weights by approximately 1~2%. To define the roles of heme-SCP in modulating body weight and gut microbiota, obese C57BL/6N mice were administered varied heme-SCP concentrations (0, 0.05, and 0.5% heme-SCP in high fat diet) for 28 days. The heme-SCP diet seemed to restrain weight gain till day 14, but the mice gained weight again later, showing no significant differences in weight. However, the heme-SCP-fed mice had stiffer and oilier bodies compared with those of the control mice, which had flabby bodies and dull coats. When mice were dissected at day 10, the obese mice fed with heme-SCP exhibited a reduction in subcutaneous fat with an increase in muscle mass. The effect of heme-SCP on the obesity-associated dyslipidemia tended to be corroborated by the blood parameters (triglyceride, total cholesterol, and C-reactive protein) at day 10, though the correlation was not clear at day 28. Notably, the heme-SCP diet altered gut microbiota, leading to the proliferation of known anti-obesity biomarkers such as Akkermansia, Alistipes, Oscillibacter, Ruminococcus, Roseburia, and Faecalibacterium. This study suggests the potential of heme-SCP as an anti-obesity supplement, which modulates serum biochemistry and gut microbiota in high-fat diet-induced obese mice.

• 한국미생물·생명공학회지
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• 제24권5호
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• pp.579-584
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• 1996

The molecular weight of the purified nucleoside oxidase estimated by gel filtration column chromatography was 480,000 and the enzyme protein was composed of four nonidentical subunits (81,000, 69,000, 32,000 and 16,000). On the basis of the visible absorption spectra and the enzymatic determination of the purified enzyme, the enzyme was supposed as a hemoprotein and also a flavoprotein containing 3 moles of FAD per I mole of enzyme. The isoelectric point of the enzyme was pH 5.1. Addition of metal salts such as 1 mM SnCl$_{2}$ and PbCl$_{2}$ into an enzyme reaction solution inhibited the enzyme activity by 94 and 90%, respectively. The enzyme activity was also lost significantly by hemoenzyme inhibitors such as NaCN and NaN$_{3}$ and flavoenzyme inhibitor, acriflavine and quinacrine. The maximal nucleoside oxidase activity was observed at pH 7.0 and 55$\circ$C. The nucleoside oxidase was relatively stable in the range of pH 5.5-9.0 and below 55$\circ$C.

• 약학회지
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• 제32권6호
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• pp.420-427
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• 1988

Post-translational modification of protein amino acid residues is a well known metabolic phenomenon. One such side chain modification, protein methylation, occur ubiquitously in nature, in organism ranging from prokaryotic to eukaryotic and the biological significance of protein methylation has begun to emerge. The observation that cytochrome C methylation facilitates the binding of this hemoprotein to mitochondria could be placed as the one of the examples along this line. However, the detail biological meaning of cytochrome C methylation is remained to be clarified. In the aspect of such reason this research was done. The results of this experiment were; 1) pure Euglena gracilis cytochrome C552 was isolated, 2) methylarginine and methylmethionine were not found in cytochrome C552 sequence, 3) however, Unknown Peak at 20.78min of retention time was found, and 4) this Unknown Peak was found only from Euglena cytochrome C552, so far.

• 한국미생물·생명공학회지
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• 제24권5호
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• pp.585-590
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• 1996

Peroxidase was purified to homogeneity from cell free extract of Flavobacterium meningosepticum. The molecular weight of the enzyme estimated by gel filtration column chromatography was 220, 000. A identical subunit (54, 000) was detected on SDS-PAGE of the enzyme. From these results, the enzyme was supposed to have four identical subunits. On the basis of the visible absorption spectra of the purified enzyme, the enzyme was a typical hemoprotein. The isoelectric point of the enzyme was 4.1. On using N-ethyl-N-(2-hydroxy-3-sulfopropyl)-m- toluidine (Toos) as a hydrogen donor, the enzyme showed optimum activity at the pH 5.5 and 50$\circ$C. The enzyme activity was inhibited by carbonyl reagent and Hg$^{2+}$ .

• Archives of Pharmacal Research
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• 제21권3호
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• pp.305-309
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• 1998

Human cytochrome P450 1A2 is one of the major cytochrome P450s in human liver. It is known to be capable of activating a number of carcinogens such as arylamines and heterocyclic amines. In order to develop the new bacterial mutagenicity test system with human P450, a full length of human P450 1A2 cDNA inserted into pCW bacterial expression vector was introduced to Escherichia coli WP2 uvrA strain which is a well-known E. coli strain for bacterial reverse mutagenicity assay. Expressed human P450 1A2 showed typical P450 hemoprotein spectra. Maximum expression was achieved at 48 hrs after incubating at $30^{\circ}C$ in terrific broth containing ampicillin, IPTG and other supplements. High level expression of P450 1A2 in E. coli WP2 uvrA membranes was determined in SDS-PAGE. The well-known mutagens 2-aminoanthracene and MElQ increased the revertant colonies of E. coli WP2 uvrA expressing human P450 1A2 without an exogenous rat hepatic post-mitochondrial supernatant (S9 fraction) in a dose-dependent manner. The results show that the functional expression of human P450 in bacterial mutagenicity tester strain will provide a useful tool for studying the mechanism of the mutagenesis and carcinogenesis of new drugs and environmental chemicals.

• 분석과학
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• 제11권1호
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• pp.73-78
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• 1998

미오글로빈 시안착물(MbCN) 단백질에 대한 NMR의 HMQC 연구는 수소와 결합된 상자기성 heme 탄소 시그날의 완전한 지정을 가능토록 해준다. 이러한 상자기성 MbCN에 대한 HMQC 실험의 적용은 heme시그날뿐만 아니라 상자기성 아미노산에 대해 결합된 수소와 탄소간의 coherence를 지정하여주며 자연존재량 $^{13}C$시그날의 지정이 모든 low-spin 상자기성 heme단백질에서도 가능하다. 이러한 시그날 지정 전략은 정자기성 영역에서 공명하는 수소 시그날의 지정을 위해 사용되는 NOE에만 의존하는것 보다 훨씬 명확한 시그날지정이 가능하다. 2,4-비닐기의 ${\alpha}$-탄소들과 7-프로피온기의 ${\beta}$-탄소에서 특이한 anti-Curie형태를 보이는 것은 그들이 heme평면에 존재하고 있지 않다는 증거가 된다. Proximal His에 의해 유도된 heme의 전자 및 자성의 비대칭은 heme탄소 시그날공명이 $25^{\circ}C$에서 250 ppm의 범위에 이르도록 한다. 이러한 heme 탄소 시그날 공명은 미오그로빈 heme의 전자구조를 분석하는데 있어서 수소 시그날의 공명보다 더욱 민감한 증거로 작용할수 있다.