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[血红素配合物对分子氧的活化作用]

[Activation of molecular oxygen by hemin complexes].

作者信息

Kühn M

出版信息

Prikl Biokhim Mikrobiol. 1982 Jul-Aug;18(4):489-98.

PMID:7122439
Abstract

This paper considers main properties, structure of the active center and the mechanism of action of cytochromes P-450 of different origin. It compares the literature data on structural models of P-450. Three hemin complexes which are functional models of P-450 were synthesized. Hemin was covalently bonded via carboxyl or methine groups with amino groups of polymethyl methacrylate-based polymers or coordination bonded via iron with imidazole containing polymethyl methacrylate. The diimidazole coordination complex showed the highest specific activity. In H2O2-dependent reactions the complex displayed V M and K M similar to those of liver microsomal cytochrome P-450. In NADPH-dependent reactions the specific activity of the complex was only 1-3% that of cytochrome P-450. The above findings as well as the electronic and EPR-spectra suggest that the complex can be regarded as a functional but not as a structural model of cytochrome P-450.

摘要

本文探讨了不同来源的细胞色素P - 450的主要性质、活性中心结构及作用机制。比较了有关P - 450结构模型的文献数据。合成了三种作为P - 450功能模型的血红素复合物。血红素通过羧基或次甲基与聚甲基丙烯酸甲酯基聚合物的氨基共价键合,或通过铁与含咪唑的聚甲基丙烯酸甲酯配位键合。双咪唑配位复合物表现出最高的比活性。在依赖过氧化氢的反应中,该复合物表现出与肝微粒体细胞色素P - 450相似的V M和K M。在依赖烟酰胺腺嘌呤二核苷酸磷酸(NADPH)的反应中,该复合物的比活性仅为细胞色素P - 450的1 - 3%。上述发现以及电子光谱和电子顺磁共振光谱表明,该复合物可被视为细胞色素P - 450的功能模型而非结构模型。

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