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首页> 外文期刊>Israel journal of chemistry >Generation of New Artificial Metalloproteins by Cofactor Modification of Native Hemoproteins
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Generation of New Artificial Metalloproteins by Cofactor Modification of Native Hemoproteins

机译：代的新人工金属离子代数余子式的修改本机Hemoproteins

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摘要

Heme can be removed from a number of native hemoproteins, thus forming corresponding apoproteins, each of which provides a site for binding of a metal complex. In one example, myoglobin, an O-2 storage protein, can be reconstituted with iron porphycene to dramatically enhance the O-2 affinity. Although it is known that myoglobin has poor enzymatic activity, the insertion of iron corrole or iron porphycene into apomyoglobin increases its H2O2-dependent peroxidase/peroxygenase activities. Furthermore, reconstitution with manganese porphycene promotes hydroxylation of an inert C-H bond. It is also of interest to insert a non-porphyrinoid complex into an apoprotein. A cavity of apocytochrome c has been found to bind a diiron carbonyl complex, serving as a functional model of diiron hydrogenase. Aponitrobindin has a rigid beta-barrel structure that provides an excellent cavity for covalently anchoring a metal complex. A rhodium complex embedded in the cavity of genetically modified nitrobindin has been found to promote stereoselective polymerization of phenylacetylene.
机译：血红素可以从许多本地删除hemoproteins,从而形成相应的载脂蛋白,每一种都提供了一个网站金属络合物的绑定。肌红蛋白,一个0 2存储蛋白质,可以与铁porphycene重组显著提高0 2的亲和力。众所周知,肌红蛋白有可怜的酶活动,corrole铁或铁的插入porphycene apomyoglobin增加了H2O2-dependent过氧化物酶/ peroxygenase活动。锰porphycene促进羟基化的惰性碳氢键。non-porphyrinoid复杂到一个脱辅基蛋白。结合腔apocytochrome c被发现一个diiron羰基复杂,作为功能模型diiron氢化酶。Aponitrobindin刚性beta-barrel结构提供了一个极好的腔共价锚定一个金属复杂。嵌入在转基因的腔促进nitrobindin被发现立体选择聚合的苯乙炔。

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