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金属茂在蛋白质修饰中的应用。四甲基环丁二烯镍醇脱氢酶的形成。

The use of metallocenes for protein modification. Formation of tetramethylcyclobutadiene nickel alcohol dehydrogenase.

作者信息

Giese R W, Kornicker W

出版信息

Biochim Biophys Acta. 1983 Jul 28;746(1-2):97-100. doi: 10.1016/0167-4838(83)90015-8.

DOI:10.1016/0167-4838(83)90015-8
PMID:6347259
Abstract

Tetramethylcyclobutadiene nickel dichloride is a dark red, half-sandwich nickel metallocene with both aqueous and organic solubility. It reacts extensively with horse liver alcohol dehydrogenase (EC 1.1.1.1), forming an orange, soluble adduct that is stable at least to moderate dialysis and essentially devoid of native zinc and also enzymatic activity. This modified enzyme contains nearly 8 mol nickel per mol and possesses a positive Cotton effect. Under the same conditions, nickel chloride has no effect on the enzyme. This illustrates the potential for half-sandwich metallocenes to provide unique reactivity and spectral characteristics for protein modification.

摘要

二氯四甲基环丁二烯合镍是一种深红色的半夹心型镍茂金属配合物,具有水相和有机相溶解性。它与马肝醇脱氢酶(EC 1.1.1.1)发生广泛反应,形成一种橙色的可溶性加合物,该加合物至少在适度透析条件下稳定,且基本不含天然锌和酶活性。这种修饰后的酶每摩尔含有近8摩尔镍,并具有正的科顿效应。在相同条件下,氯化镍对该酶无影响。这说明了半夹心型金属茂配合物为蛋白质修饰提供独特反应性和光谱特征的潜力。

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