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去除2型铜(II)的日本漆树漆酶的光学性质。2型铜(II)在330nm发色团中的作用。

Optical properties of japanese-lacquer-tree (Rhus vernicifera) laccase depleted of type 2 copper(II). Involvement of type-2 copper(II) in the 330nm chromophore.

作者信息

Morpurgo L, Graziani M T, Finazzi-Agrò A, Rotilio G, Mondovì B

出版信息

Biochem J. 1980 May 1;187(2):361-6. doi: 10.1042/bj1870361.

Abstract
  1. Spectroscopic and functional properties of Japanese-lacquer-tree (Rhus vernicifera) laccase were re-investigated, with special emphasis on the relationships between the different types of copper centres (Types 1, 2, and 3). 2. On removal of the Type 2 Cu(II), a decrease of absorbance occurred in the wavelength region above 650 nm (delta epsilon 750 = 300 M-1 . cm-1) and around 330 nm (delta episom 330 up to 2200 M-1 . cm-1). 3. Reductive titrations with ascorbic acid or ferrocyanide showed that the electron-accepting capacity of the partial apoprotein is one electron-equivalent lower than that of the native protein, i.e. the protein two-electron acceptor is present in the oxidized state in spite of absorbance loss at 330 nm. 4. The 330 nm chromophore apparently depends on the presence of both the Type 2 and the Type 3 copper in the oxidized state. 5. This finding may have implications in the relative location of Type 2 and 3 copper centres and on the redox behaviour of laccase.
摘要
  1. 对漆树漆酶的光谱和功能特性进行了重新研究,特别强调了不同类型铜中心(1型、2型和3型)之间的关系。2. 去除2型Cu(II)后,在650 nm以上波长区域(Δε750 = 300 M-1·cm-1)和330 nm左右(Δε330高达2200 M-1·cm-1)吸光度降低。3. 用抗坏血酸或亚铁氰化物进行的还原滴定表明,部分脱辅基蛋白的电子接受能力比天然蛋白低一个电子当量,即尽管在330 nm处吸光度下降,但蛋白质双电子受体仍以氧化态存在。4. 330 nm发色团显然取决于氧化态的2型和3型铜的同时存在。5. 这一发现可能对2型和3型铜中心的相对位置以及漆酶的氧化还原行为有影响。

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Studies of the metal sites of copper proteins. Ligands of copper in hemocuprein.
Biochemistry. 1971 Feb 16;10(4):616-21. doi: 10.1021/bi00780a011.
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Eur J Biochem. 1973 May 2;34(3):434-9. doi: 10.1111/j.1432-1033.1973.tb02776.x.

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