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The role of cupric in maintaining the structure of CopC 被引量:4

The role of cupric in maintaining the structure of CopC
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摘要 The CopC protein from pseudomonas syringae pathovar tomato is expressed as one of four proteins encoded by the operon CopABCD that is responsible for copper resistance. And there are one trypto-phan (83), one tyrosine (79), and three phenylalanines (35, 43, 99) in apoCopC. The fluorescence peak of apoCopC is located near 320 nm, and the peak shifts toward 353 nm in the presence of 10 mmol·L^(-1) urea with excitation at 280 nm. Using urea as a chemical agent, the conformational stabilities of apoCopC and Cu_N^(2+) -CopC were monitored by fluorescence spectrum in 20 mmol·L^(-1) phosphate buffer and 100 mmol·L^(-1) sodium chloride at pH 6.0. The free energy of stabilization for apoCopC and Cu_N^(2+)-CopC is 16.29±0.65 kJ·mol^(-1) and 26.26±0.35 kJ·mol^(-1), respectively. The distance between the tryptophan residue and the Cu^(2+) in Cu_N^(2+) -CopC has been studied by observing Frster type nonradia-tive energy transfer. And it is calculated to be 11.6 . The CopC protein from pseudomonas syringae pathovar tomato is expressed as one of four proteins encoded by the operon CopABCD that is responsible for copper resistance. And there are one tryptophan (83), one tyrosine (79), and three phenylalanines (35, 43, 99) in apoCopC. The fluorescence peak of apoCopC is located near 320 nm, and the peak shifts toward 353 nm in the presence of 10 mol·L^-1 urea with excitation at 280 nm. Using urea as a chemical agent, the conformational stabilities of apoCopC and CuN^2+ . CopC were monitored by fluorescence spectrum in 20 mmol·L^-1 phosphate buffer and 100 mmol·L^-1 sodium chloride at pH 6.0. The free energy of stabilization for apoCopC and CuN^2+-CopC is 16.29±0.65 kJ·mol^-1 and 26.26±0.35 kJ·mol^-1, respectively. The distance between the tryptophan residue and the Cu^2+ in CuN^2+ .CopC has been studied by observing Foerster type nonradiative energy transfer. And it is calculated to be 11.6 A.
出处 《Chinese Science Bulletin》 SCIE EI CAS 2007年第6期743-747,共5页
基金 Supported by the National Natural Science Foundation of China (Grant No.20371031) the Natural Science Foundation of Shanxi Province (Grant No.20031017)
关键词 二价铜 CopC 蛋白质结构 构象稳定性 作用 尿素变性 apoCopC, CU2N^2+-CopC, urea, spectra
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  • 1Pena M M O,Lee J,Thiele D J.Critical review a delicate balance: Homeostatic control of copper uptake and distribution[].The Journal of Nutrition.1999
  • 2O’Hara P,Yeh S M,Meares C F.Distance between metal-binding sites in transferring: energy transfer from bound terbium (Ⅲ ) to iron (Ⅲ ) or manganese (Ⅲ )[].Biochemistry.1981
  • 3Matei E,Miron S,Blouquit Y,et al.C-terminal half of human centrin 2 behaves like a regulatory EF-hand domain[].Biochemistry.2003
  • 4Pace C N.Determination and analysis of urea and guanidine hydrchloride denaturation curves[].Methods in Enzymology.1986
  • 5Yang B S,Yang P.Interaction between rare earth ions and human se-rum albumin[].Acta Biochimica et Biophysica.1988
  • 6Arnesano F,Banci L,Bertini I,et al.Solution structure of CopC: A cupredoxin-like protein involved in copper homeostasis[].Structure.2002
  • 7PANG Erguo ZHAO Yaqin YANG Binsheng.Fluorescence study on the interaction between apoCopC and cupric[J].Chinese Science Bulletin,2005,50(20):2302-2305. 被引量:5
  • 8Burstein E A,Vedenkina N S,Ivkova M N.Fluorescence and the lo-cation of tryptophan residues in protein molecules[].Photochemical and Photobiological.1973
  • 9Koay M,Zhang L Y,Yang B S,et al.CopC protein from pseudomonas syringae: Intermolecular transfer of copper from both the copper(I) and copper(II) sites[].Inorganic Chemistry.2005
  • 10Arnesano F,Banci L,Bertini I,et al.A redox switch in CopC: An in-triguing copper trafficking protein that binds copper (Ⅰ ) and copper (Ⅱ ) at different sites[].Proceedings of the National Academy of Sciences of the United States of America.2003

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