• Applied Biological Chemistry
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• 제46권1호
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• pp.7-11
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• 2003

감자 polyphenol oxidase의 구리결합지역 DNA와 histidine 다량 함유 인공 펩타이드를 암호화하는 DNA를 대장균 벡터에 각각 클로닝하여 발현시킨 후 대장균 내의 구리함량 증감을 조사하였다. Polyphenol oxidase의 구리결합지역 DNA를 포함하는 PPOCBpET32 벡터를 함유하는 균주의 경우는 벡터를 함유하지 않는 대장균 대조구보다 오히려 구리 함량이 약간 감소하여 약 600ppm의 간을 보여주어, 감자 polyphenol oxidase 구리결합지역의 대장균 내에서의 발현이 구리 함량 증가에 기여하지 못함을 알 수 있었다. 반면에 한 개의 hexahistidine 단위 DNA를 포함하는 pET28a 벡터 함유 대장균 균주를 knamycin 미첨가 배지에서 배양한 경우에는 구리 함량이 약 2,500ppm으로 높게 나타났다. 한편 hexahistidine 9개로 구성된 polyhistidine을 암호화하는 DNA를 포함하는 pET-his 벡터 함유 균주를 kanamycin 미첨가 배지에서 배양한 경우에 구리함량이 약 3,200ppm으로 나타나, 하나의 hexahistidine 단위만 발현하는 균주와 비교하여 구리함량이 약 30% 증가됨을 알 수 있었다.

• The Korean Journal of Ecology
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• 제21권3호
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• pp.217-224
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• 1998

The heavy metal concentrations of seawater collected from the Onsan coastal zone in February and July 1996 and mussels(Mytilus edulis) in February 1997 were analysed. The concentrations of cadmium in seawater were in the range of 0.008-2.988 ${\mu}g/L$, while the ranges of copper and zinc concentrations were 0.08-2.55, and 0.21-35.12 ${\mu}g/L$, respectively. The metal concentrations decreased gradually with increasing distances from Daejeong stream, indicating that this stream was the major source of heavy metal input into the Onsan coastal zone. The concentrations of cadmium, copper and zinc in mussels were in the ranges of 1.40-25.09, 8.5-64.5, and 46.8-291.2 ${\mu}g/g$, respectively. The metal concentrations decreased gradually with increasing distances from Daejeong stream. Among organs of mussels, gill showed the highest concentrations of cadmium and the digestive gland showed the highest concentrations of copper and for zine the kidney showed the highest concentrations. The digestive gland and kidney revealed high proportion of cadmium in cytosolic fraction and the percentage of copper was high in the kidney and that of zine was high in the digestive gland. Metal-binding protein of mussels collected from the mouth of Daejeong stream was separated, using gel-filtration chromatography. In the kidney and gill of mussels, most of cadmium was associated with metal-binding protein. In contrast, most of the metal in the digestive gland and remaining tissues is bound to high molecular weight protein rather than metal-binding protein.

• 한국자기공명학회논문지
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• 제20권3호
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• pp.76-81
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• 2016

Copper is an elemental ion in living organisms. CopP from Helicobacter Pylori (HpCopP) is a copper(I)-binding protein and was suggested as regulator of copper metabolism in vivo. Previously, the metal binding property of HpCopP for Ag(I), Cu(I), and Cu(II) as well as the tertiary structure of HpCopP was shown. In this study, the dynamic profiles of HpCopP depending on metal binding were studied using ${^1H}-^{15}N$ steady-state NOE analysis. The heteroNOE experiment was performed for apo-CopP or metal-bound CopP. The obtained NOE values were analyzed and compared to figure out the effect of metals on the structural flexibility of HpCopP. As a result, Ag(I) and Cu(I) ions improved the rigidity of the structure while Cu(II) ion increased the flexibility of the structure, suggesting the oxidation of the CXXC motif decreases the structural stability of HpCopP.

• Advances in Traditional Medicine
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• 제7권2호
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• pp.171-181
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• 2007

Metal binding activity of the pectin samples with different physicochemical properties was studied. It was found that in vitro copper binding capacity of pectins is depending on the following factors: degree of esterification, content of non-methylated anhydrogalacturonic acid, and pH of solution. There was found that the maximum copper uptake capacity increases correspondingly to reduction of the degree of esterification of pectin, rise of the non-methylated anhydrogalacturnic acid content and the solution pH. It is proposed to use for standardization of pectin samples such parameters as the degree of esterification, content of anhydrogalacturonic acid, and intrinsic viscosity.

• 미생물학회지
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• 제35권1호
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• pp.25-27
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• 1999

Coprinus congregatus 의 염색체 DNA를 주형으로 사용하고 균류 laccase에서 잘 보존된 copper binding region의 염기서열을 primer 로 사용하여 PCR을 수행한 결과 144 bp 길이의 laccase 유전자 일부를 cloning 하였다. 이의 염기서열을 분석한 결과 다른 균류의 lacacse 와 60-69% 정도의상동성을 보였으며 추정된 아미노산 서열은 68-75%의 상동성을 보였다.

• Journal of Microbiology and Biotechnology
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• 제31권2호
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• pp.233-239
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• 2021

Cyanobacteriochromes (CBCRs) are phytochrome-related photoreceptor proteins in cyanobacteria and cover a wide spectral range from ultraviolet to far-red. A single GAF domain that they contain can bind bilin(s) autocatalytically via heterologous recombination and then fluoresce, with potential applications as biomarkers and biosensors. Here, we report that a novel red/green CBCR GAF domain, SPI1085g2 from Spirulina subsalsa, covalently binds both phycocyanobilin (PCB) and phycoerythrobilin (PEB). The PCB-binding GAF domain exhibited canonical red/green photoconversion with weak fluorescence emission. However, the PEB-binding GAF domain, SPI1085g2-PEB, exhibited an intense orange fluorescence (λabs.max = 520 nm, λfluor.max = 555 nm), with a fluorescence quantum yield close to 1.0. The fluorescence of SPI1085g2-PEB was selectively and instantaneously quenched by copper ions in a concentration-dependent manner and exhibited reversibility upon treatment with the metal chelator EDTA. This study identified a novel PEB-binding cyanobacteriochrome-based fluorescent protein with the highest quantum yield reported to date and suggests its potential as a biosensor for the rapid detection of copper ions.

• 대한전자공학회논문지
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• 제25권1호
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• pp.27-32
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• 1988

Electron Spectroscopy for Chemical Analysis(ESCA) allowes the determination of the elemental composition and the bonding state of the surface atomes in the interface between two materials. In the binding energies of ESCA spectrum, there are zero error, voltage scaling error and random error. Accurate analysis of the intensity energy response functions and accurate calibration of the energy scale are essential to use X-ray photoelectron spectron meter. At the results of the calibration of the ESCA spectra in the copper and cordierite (Mg2Al4Si5kO18) interfaces, the errors relative to the copper are -3.03 eV for the zero error -z,-197 ppm for the voltage scaling error -V and 6.9 meV for the random error -R. The method of the calibration is able to apply for the binding energy calibration of the another ESCA spectra.

• Bulletin of the Korean Chemical Society
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• 제26권7호
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• pp.1051-1056
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• 2005

The interaction of bovine carbonic anhydrase II with copper ions was studied by isothermal titration microcalorimetry, circular dichroism, UV spectrophotometry and temperature scanning spectrophotometry methods at 27 ${^{\circ}C}$ in Tris buffer solution at pH = 7.5. It was indicated that there are three non-identical different binding sites on carbonic anhydrase for $Cu^{2+}$. The binding of copper ions is exothermic and can induce some minor changes in the secondary and tertiary structure of the enzyme, which does not unfold it, but can result in a decrease in both activity and stability of the enzyme.

• Bulletin of the Korean Chemical Society
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• 제34권6호
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• pp.1875-1878
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• 2013

• Molecules and Cells
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• 제37권2호
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• pp.100-108
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• 2014

Salmonella enterica serovar Typhimurium (S. Typhimurium) is an intracellular pathogen that has evolved to survive in the phagosome of macrophages. The periplasmic copper-binding protein CueP was initially known to confer copper resistance to S. Typhimurium. Crystal structure and biochemical studies on CueP revealed a putative copper binding site surrounded by the conserved cysteine and histidine residues. A recent study reported that CueP supplies copper ions to periplasmic Cu,Zn-superoxide dismutase (SodCII) at a low copper concentration and thus enables the sustained SodCII activity in the periplasm. In this study, we investigated the role of CueP in copper resistance at a high copper concentration. We observed that the survival of a cueP-deleted strain of Salmonella in macrophage phagosome was significantly reduced. Subsequent biochemical experiments revealed that CueP specifically mediates the reduction of copper ion using electrons released during the formation of the disulfide bond. We observed that the copper ion-mediated Fenton reaction in the presence of hydrogen peroxide was blocked by CueP. This study provides insight into how CueP confers copper resistance to S. Typhimurium in copper-rich environments such as the phagosome of macrophages.