copper protein

銅蛋白質

WordNet

1. coat with a layer of copper
2. a ductile malleable reddish-brown corrosion-resistant diamagnetic metallic element; occurs in various minerals but is the only metal that occurs abundantly in large masses; used as an electrical and thermal conductor (同)Cu, atomic number 29
3. a copper penny
4. a reddish-brown color resembling the color of polished copper (同)copper color
5. any of various small butterflies of the family Lycaenidae having coppery wings
6. any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"

PrepTutorEJDIC

1. 〈U〉『銅』(化学記号は『Cu』) / 〈C〉《英話》銅貨 / 〈C〉銅製品,銅器;《英》(先濯用)銅の大がま / 〈U〉赤銅色 / 銅[製]の / 赤銅色の / …‘に'をかぶせる,銅板を張る
2. ポリ公
3. 蛋白(たんばく)質

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/05/06 07:53:15」(JST)

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Copper proteins are proteins that contain one or more copper ions as prosthetic groups. The metal centres in the copper proteins can be classified into several types:

• Type I copper centres (T1Cu) are characterized by a single copper atom coordinated by two histidine residues and a cysteine residue in a trigonal planar structure, and a variable axial ligand. In class I T1Cu proteins (e.g. amicyanin, plastocyanin and pseudoazurin) the axial ligand is the sulfur of methionine, whereas aminoacids other than methionine (e.g. glutamine) give rise to class II T1Cu copper proteins. Azurins contain the third type of T1Cu centres: besides a methionine in one axial position, they contain a second axial ligand (a carbonyl group of a glycine residue). T1Cu-containing proteins are usually called "cupredoxins", and show similar three-dimensional structures, relatively high reduction potentials (> 250 mV), and strong absorption near 600 nm (due to S→Cu charge transfer), which usually gives rise to a blue colour. Cupredoxins are therefore often called "blue copper proteins". This may be misleading, since some T1Cu centres also absorb around 460 nm and are therefore green. When studied by EPR spectroscopy, T1Cu centres show small hyperfine splittings in the parallel region of the spectrum (compared to common copper coordination compounds).
• Type II copper centres (T2Cu) exhibit a square planar coordination by N or N/O ligands. They exhibit an axial EPR spectrum with copper hyperfine splitting in the parallel region similar to that observed in regular copper coordination compounds. Since no sulfur ligation is present, the optical spectra of these centres lack distinctive features. T2Cu centres occur in enzymes, where they assist in oxidations or oxygenations.
• Type III copper centres (T3Cu) consist of a pair of copper centres, each coordinated by three histidine residues. These proteins exhibit no EPR signal due to strong antiferromagnetic coupling (i.e. spin pairing) between the two S = 1/2 metal ions due to their covalent overlap with a bridging ligand. These centres are present in some oxidases and oxygen-transporting proteins (e.g. hemocyanin and tyrosinase).
• Binuclear Copper A centres (Cu_A) are found in cytochrome c oxidase and nitrous-oxide reductase (EC 1.7.99.6). The two copper atoms are coordinated by two histidines, one methionine, a protein backbone carbonyl oxygen, and two bridging cysteine residues.
• Copper B centres (Cu_B) are found in cytochrome c oxidase. The copper atom is coordinated by three histidines in trigonal pyramidal geometry.
• Tetranuclear Copper Z centre (Cu_Z) is found in nitrous-oxide reductase. The four copper atoms are coordinated by seven histidine residues and bridged by a sulfur atom.

See also

• Copper in health

References

UpToDate Contents

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• 1. 食物中の微量ミネラルの概要 overview of dietary trace minerals
• 2. 銅欠乏性脊髄神経障害 copper deficiency myeloneuropathy
• 3. ウィルソン病：疫学および病因 wilson disease epidemiology and pathogenesis
• 4. プリオンの生物学および遺伝学 biology and genetics of prions
• 5. 鉄のバランス調節 regulation of iron balance

English Journal

• Molecular cloning, characterization of copper/zinc superoxide dismutase and expression analysis of stress-responsive genes from Eisenia fetida against dietary zinc oxide.

• Xiong W, Bai L, Muhammad RU, Zou M, Sun Y.AbstractThe full length cDNA of copper/zinc superoxide dismutase (Cu/Zn-SOD) from Eisenia fetida (E. fetida) was cloned (GenBank accession no. JN579648). Sequence characterization revealed that the cDNA contained characteristic Cu/Zn-SOD family signatures ((45)GFHVHEFGDNT(55) and (138)GNAGGRLACGVI(149)), cysteines (Cys-58 and-146) predicted to form one disulphide bond, Cu-binding (His-47, -49, -64 and -120) and Zn-binding (His-64, -72, -81 and Asp-84). They were essential for the structure and function of Cu/Zn-SOD. Differential expression of stress-responsive genes like Cu/Zn-SOD, catalase (CAT), heat shock protein 70 (Hsp70) and metallothionein (MT) was applied as potential biomarkers to assess their efficacy for the ecotoxicological effects of dietary zinc oxide (ZnO) on E. fetida. The results showed that the expression of Cu/Zn-SOD and MT increased to reach the highest levels of 6.22 and 7.68 fold in a dose-dependent manner at day 10 respectively. The highest expression of 3.03 fold of CAT was registered at day 10. The transient expression of Hsp70 without consistent time- or/and dose-dependent was observed. It implied that the transcriptional patterns of Cu/Zn-SOD, CAT and MT could serve as early warning signals in ecotoxicological assessment of dietary ZnO on earthworms while the expression of Hsp70 was not well done, which is helpful to monitoring and regulation of ZnO in veterinary application.
• Comparative biochemistry and physiology. Toxicology & pharmacology : CBP.Comp Biochem Physiol C Toxicol Pharmacol.2012 Mar;155(2):416-22. Epub 2011 Nov 26.
• The full length cDNA of copper/zinc superoxide dismutase (Cu/Zn-SOD) from Eisenia fetida (E. fetida) was cloned (GenBank accession no. JN579648). Sequence characterization revealed that the cDNA contained characteristic Cu/Zn-SOD family signatures ((45)GFHVHEFGDNT(55) and (138)GNAGGRLACGVI(149)), cy
• PMID 22137962

• Susceptibility to oxidative stress and modulated expression of antioxidant genes in the copper-exposed polychaete Perinereis nuntia.

• Won EJ, Rhee JS, Kim RO, Ra K, Kim KT, Shin KH, Lee JS.SourceDepartment of Environmental Marine Sciences, College of Science and Technology, Hanyang University, Ansan 426-791, South Korea; Department of Chemistry, College of Natural Sciences, Hanyang University, Seoul 133-791, South Korea.
• Comparative biochemistry and physiology. Toxicology & pharmacology : CBP.Comp Biochem Physiol C Toxicol Pharmacol.2012 Mar;155(2):344-51. Epub 2011 Oct 20.
• To identify and evaluate potentially useful biomarkers for oxidative stress as early warning indices in the polychaete, Perinereis nuntia, we exposed P. nuntia to copper (Cu) and measured several biomarker enzymes (glutathione S-transferase; GST, glutathione peroxidase; GPx, Metallothionein-like pro
• PMID 22037546

Japanese Journal

• Characterization of a putative chromosome segregation and condensation protein (ScpB) in an acidophilic iron‒oxidizing bacterium Acidithiobacillus ferrooxidans

• 上村 一雄,長田 臨,菊本 愛生,Sharmin Sultana,若井 暁,金尾 忠芳
• 岡山大学農学部学術報告 104, 5-12, 2015-02-01
• … Acidithiobacillus ferrooxidans is one of the most widely used microorganisms in bioleaching operations to recover copper from low-grade copper sulfide. … A gene encoding a putative chromosome segregation and condensation protein (ScpB) with ahelix-turn-helix motif was found in the upstream region of sulfide : quinone oxidoreductase gene, whose expression was up-regulated in cells grown in sulfur and tetrathionate. …
• NAID 120005537568

• Reflectometric interference spectroscopy-based immunosensing using immobilized antibody via His-tagged recombinant protein A(BIOCHEMICAL ENGINEERING)

• Choi Hyung Woo,Sakata Yasuhiko,Ooya Tooru [他],Takeuchi Toshifumi
• Journal of bioscience and bioengineering 119(2), 195-199, 2015-02
• … The proposed approach demonstrated in this study provides an immunosensing system based on refiectomenic interference spectroscopy (RIfS) in combination with an antibody immobilization method using histidine-tagged recombinant protein A. … Carboxymethyldextran (CMD) was immobilized on a 3-aminopropyltriethoxysilane-treated a silicon nitride-coated silicon wafer, followed by chelating histidine-tagged recombinant protein A with copper (II) ions. …
• NAID 110009922581

• The Allosteric Regulation of Axial/Rhombic Population in a "Type 1" Copper Site: Multi-edge X-ray Absorption Spectroscopic and Density Functional Studies of Pseudoazurin

• Yamaguchi Takahide,Yano Junko,Yachandra Vittal K.,Nihei Yuko,Togashi Hiromi,Szilagyi Robert K.,Kohzuma Takamitsu
• Bulletin of the Chemical Society of Japan advpub(0), 2015
• … The co-existence of "axial" and "rhombic" coordination environments have been demonstrated in a "Type 1" copper site of Pseudoazurin. … This observation opens up previously not considered interpretations for the relationship between geometry and electronic structure of the four coordinate copper site. …
• NAID 130005096017

Related Links

• copper protein - definition of copper protein by Medical dictionary

cop·per pro·tein a protein containing one or more copper ions; for example, cytochrome c oxidase, phenol oxidase.

• copper protein - Definition

copper protein definition from the mondofacto online medical dictionary ... help contact sitemap copper protein definition home dictionary word tools courses study skills forum about us Search dictionary help copper protein medical ...

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copper protein

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