What are the structural features of the active site that define binuclear copper proteins function?
暂无分享,去创建一个
[1] L. Bubacco,et al. Spectroscopic Characterization of the Electronic Changes in the Active Site of Streptomyces antibioticus Tyrosinase upon Binding of Transition State Analogue Inhibitors* , 2003, The Journal of Biological Chemistry.
[2] L. Bubacco,et al. Structural Basis and Mechanism of the Inhibition of the Type-3 Copper Protein Tyrosinase from Streptomyces antibioticusby Halide Ions* 210 , 2002, The Journal of Biological Chemistry.
[3] L. Bubacco,et al. Oxidized derivatives of Octopus vulgaris and Carcinus aestuarii hemocyanins at pH 7.5 and related models by x-ray absorption spectroscopy. , 2002, Biophysical journal.
[4] H. Decker,et al. Cops and robbers: putative evolution of copper oxygen-binding proteins. , 2000, The Journal of experimental biology.
[5] L. Bubacco,et al. EPR study of the dinuclear active copper site of tyrosinase from Streptomyces antibioticus , 2000, FEBS letters.
[6] L. Bubacco,et al. EPR study of the dinuclear active site of Tyrosinase from Streptomyces antibioticus , 2000 .
[7] L. Bubacco,et al. 1H NMR spectroscopy of the binuclear Cu(II) active site of Streptomyces antibioticus tyrosinase , 1999, FEBS letters.
[8] L. Bubacco,et al. Characterisation by proton NMR spectroscopy of the binuclear site of Streptomyces antibioticus Tyrosinase , 1999 .
[9] B. Krebs,et al. Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes (Ipomoea batatas) containing a type‐3 dicopper center 1 , 1998, FEBS letters.
[10] H. Decker,et al. Tarantula Hemocyanin Shows Phenoloxidase Activity* , 1998, The Journal of Biological Chemistry.
[11] S. Alvarez,et al. Structural Modeling and Magneto-Structural Correlations for Hydroxo-Bridged Copper(II) Binuclear Complexes. , 1997, Inorganic chemistry.
[12] Edward I. Solomon,et al. ELECTRONIC STRUCTURES OF ACTIVE SITES IN COPPER PROTEINS : CONTRIBUTIONS TO REACTIVITY , 1992 .
[13] W G Hol,et al. Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution. , 1994, Journal of molecular biology.