Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes (Ipomoea batatas) containing a type-3 dicopper center

被引：150
作者：
Eicken, C
Zippel, F
Büldt-Karentzopoulos, K
Krebs, B
机构：
[1] Univ Munster, Inst Anorgan Chem, D-48149 Munster, Germany
[2] Univ Munster, Inst Biochem, D-48149 Munster, Germany
来源：
FEBS LETTERS | 1998年 / 436卷 / 02期
关键词：
catechol oxidase; dicopper enzyme; EXAFS; N-terminal sequence; Ipomoea batatas;
D O I：
10.1016/S0014-5793(98)01113-2
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Two catechol oxidases have been isolated from sweet potatoes (Ipomoea batatas) and purified to homogeneity. The two isozymes have been characterized by EXAFS, EPR-, UV/Vis-spectroscopy, isoelectric focusing, and MALDI-MS and have been shown to contain a dinuclear copper center. Both are monomers with a molecular mass of 39 kDa and 40 kDa, respectively. Substrate specificity and NH2-terminal sequences have been determined. EXAFS data for the 39 kDa enzyme reveal a coordination number of four for each Cu in the resting form and suggest a Cu(II)-Cu(II) distance of 2.9 Angstrom for the native met form and 3.8 Angstrom for the oxy form. (C) 1998 Federation of European Biochemical Societies.
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收藏
页码：293 / 299
页数：7
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