鏻化合物作为牛血清胺氧化酶的新型特异性抑制剂。
Phosphonium compounds as new and specific inhibitors of bovine serum amine oxidase.
作者信息
Di Paolo Maria Luisa, Lunelli Michele, Scarpa Marina, Rigo Adelio
机构信息
Dipartimento di Chimica Biologica, Università di Padova, Via G. Colombo 3, 35121 Padova, Italy.
出版信息
Biochem J. 2004 Dec 15;384(Pt 3):551-8. doi: 10.1042/BJ20031883.
TPP+ (tetraphenylphosphonium ion) and its analogues were found to act as powerful competitive inhibitors of BSAO (bovine serum amine oxidase). The binding of this new class of inhibitors to BSAO was characterized by kinetic measurements. TPP+ can bind to the BSAO active site by hydrophobic and by coulombian interactions. The binding probably occurs in the region of the 'cation-binding site'[Di Paolo, Scarpa, Corazza, Stevanato and Rigo (2002) Biophys. J. 83, 2231-2239]. Under physiological conditions, the association constant of TPP+ for this site is higher than 10(6) M(-1), the change of enthalpy being the main free-energy term controlling binding. Analysis of the relationships between substrate structure and extent of inhibition by TPP+ reveals some new molecular features of the BSAO active site.
四苯基鏻离子（TPP+）及其类似物被发现是牛血清胺氧化酶（BSAO）的强效竞争性抑制剂。通过动力学测量对这类新型抑制剂与BSAO的结合进行了表征。TPP+可通过疏水作用和库仑相互作用与BSAO活性位点结合。这种结合可能发生在“阳离子结合位点”区域[迪保罗、斯卡尔帕、科拉扎、斯特凡纳托和里戈（2002年）《生物物理杂志》83卷，2231 - 2239页]。在生理条件下，TPP+与该位点的缔合常数高于10⁶ M⁻¹，焓变是控制结合的主要自由能项。对底物结构与TPP+抑制程度之间关系的分析揭示了BSAO活性位点的一些新分子特征。
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