Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes (Ipomoea batatas) containing a type-3 dicopper center
作者： Christoph Eicken , Frank Zippel , Klaudia Büldt-Karentzopoulos , Bernt Krebs
DOI: 10.1016/S0014-5793(98)01113-2
关键词: Polyacrylamide gel electrophoresis 、 Ipomoea 、 Catechol 、 Enzyme 、 Catechol oxidase 、 Isozyme 、 Molecular mass 、 Stereochemistry 、 Isoelectric focusing 、 Chemistry
摘要: Two catechol oxidases have been isolated from sweet potatoes (Ipomoea batatas) and purified to homogeneity. The two isozymes characterized by EXAFS, EPR-, UV/Vis-spectroscopy, isoelectric focusing, MALDI-MS shown contain a dinuclear copper center. Both are monomers with molecular mass of 39 kDa 40 kDa, respectively. Substrate specificity NH2-terminal sequences determined. EXAFS data for the enzyme reveal coordination number four each Cu in resting form suggest Cu(II)-Cu(II) distance 2.9 A native met 3.8 oxy form.
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sci-hub.se 参考文章(42)
S.P. Cramer, O. Tench, M. Yocum, G.N. George, A 13-element Ge detector for fluorescence EXAFS Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment. ,vol. 266, pp. 586- 591 ,(1988) , 10.1016/0168-9002(88)90449-4
G.L. Woolery, L. Powers, M. Winkler, E.I. Solomon, K. Lerch, T.G. Spiro, Extended X-ray absorption fine structure study of the coupled binuclear copper active site of tyrosinase from Neurospora crassa Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. ,vol. 788, pp. 155- 161 ,(1984) , 10.1016/0167-4838(84)90257-7
Nobumasa Kitajima, Kiyoshi Fujisawa, Chisato Fujimoto, Yoshihiko Morooka, Shinji Hashimoto, Teizo Kitagawa, Koshiro Toriumi, Kazuyuki Tatsumi, Akira Nakamura, A new model for dioxygen binding in hemocyanin. Synthesis, characterization, and molecular structure of the .mu.-.eta.2:.eta.2 peroxo dinuclear copper(II) complexes, [Cu(HB(3,5-R2pz)3)]2(O2) (R = isopropyl and Ph) Journal of the American Chemical Society. ,vol. 114, pp. 1277- 1291 ,(1992) , 10.1021/JA00030A025
B. J. DEVERALL, Phenolase and Pectic Enzyme Activity in the Chocolate Spot Disease of Beans Nature. ,vol. 189, pp. 311- 311 ,(1961) , 10.1038/189311A0
U. K. LAEMMLI, Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Nature. ,vol. 227, pp. 680- 685 ,(1970) , 10.1038/227680A0
W. P. J. Gaykema, W. G. J. Hol, J. M. Vereijken, N. M. Soeter, H. J. Bak, J. J. Beintema, 3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin Nature. ,vol. 309, pp. 23- 29 ,(1984) , 10.1038/309023A0
B G Malmstrom, Enzymology of Oxygen Annual Review of Biochemistry. ,vol. 51, pp. 21- 59 ,(1982) , 10.1146/ANNUREV.BI.51.070182.000321
Richard A Engh, Robert Huber, None, Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement Acta Crystallographica Section A. ,vol. 47, pp. 392- 400 ,(1991) , 10.1107/S0108767391001071
MM Bradford, None, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Analytical Biochemistry. ,vol. 72, pp. 248- 254 ,(1976) , 10.1016/0003-2697(76)90527-3
Martin G. Peter, Chemical Modifications of Biopolymers by Quinones and Quinone Methides Angewandte Chemie. ,vol. 28, pp. 555- 570 ,(1989) , 10.1002/ANIE.198905551