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酵母铜硫蛋白可通过直接的一价铜转移机制,从2型铜缺失的酶中重构日本漆树漆酶。

Yeast copper-thionein can reconstitute the Japanese-lacquer-tree (Rhus vernicifera) laccase from the Type 2-copper-depleted enzyme via a direct copper(I)-transfer mechanism.

作者信息

Morpurgo L, Hartmann H J, Desideri A, Weser U, Rotilio G

出版信息

Biochem J. 1983 May 1;211(2):515-7. doi: 10.1042/bj2110515.

Abstract

The Type 2-Cu-depleted laccase from the Japanese lacquer tree (Rhus vernicifera) can be reconstituted with CuSO4 aerobically and much more rapidly and efficiently under anaerobic reducing conditions. This is to be related to a more favourable conformation of a laccase in the reduced state, rather than to reduction of the metal ion. In fact, reconstitution with Cu(I)-thionein from baker's yeast (Saccharomyces cerevisiae) only proceeds under anaerobic reducing conditions, via a direct transfer of Cu(I).

摘要

来自漆树(漆树)的2型贫铜漆酶可以在有氧条件下用硫酸铜进行重构,并且在厌氧还原条件下重构速度更快、效率更高。这与还原态漆酶更有利的构象有关,而不是与金属离子的还原有关。事实上,用来自面包酵母(酿酒酵母)的铜(I)-硫蛋白进行重构仅在厌氧还原条件下通过铜(I)的直接转移进行。

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Copper transfer between Neurospora copper metallothionein and type 3 copper apoproteins.
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