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[青霉活力过氧化氢酶辅基的光谱特性]

[Spectral properties of the prosthetic group of Penicillium vitale catalase].

作者信息

Mironenko N I, Demchenko A P, Dertiar' R G, Gulyi M F

出版信息

Ukr Biokhim Zh (1978). 1978 Mar-Apr;50(2):234-9.

PMID:664035
Abstract

Differences in the absorption spectrum of the Penicillum vitale catalase in the visible region as compared to the absorption spectrum for catalase of animal origin are established to be due to the prosthetic group of the enzyme. A molecule of P. vitale catalase is determined to contain 0.051 +/- 0.0003% of iron. It corresponds to two iron atoms per enzyme molecule and to a twice as low content of iron as in a molecule of the bovine liver catalase. An assumption is advanced that the P. vitale catalase contains two hemin groups located in two protein subunits.

摘要

已确定,与动物源过氧化氢酶的吸收光谱相比,产紫青霉过氧化氢酶在可见光区域的吸收光谱差异是由于该酶的辅基所致。经测定,产紫青霉过氧化氢酶分子含铁0.051±0.0003%。这相当于每个酶分子含有两个铁原子,且铁含量是牛肝过氧化氢酶分子中铁含量的一半。有人提出一种假设,即产紫青霉过氧化氢酶在两个蛋白质亚基中含有两个血红素基团。

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