Leishmania major peroxidase is a cytochrome c peroxidase.
Leishmania major peroxidase is a cytochrome c peroxidase.
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DOI：
10.1021/bi300169x
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发表时间：
2012-03-27
期刊：
影响因子：
2.9
通讯作者：
Poulos TL
中科院分区：
文献类型：
--
作者：
Jasion VS;Poulos TL
硕大利什曼原虫过氧化物酶（LmP）具有抗坏血酸和细胞色素c过氧化物酶活性。我们以前的研究结果表明，LmP对马心细胞色素c的活性比抗坏血酸高得多，这表明细胞色素c可能是生物学上重要的底物。为了阐明LmP的生物学功能，我们对硕大利什曼原虫细胞色素c（LmCytc）进行了重组表达、纯化和晶体结构测定。与其他细胞色素c一样，LmCytc具有围绕暴露的血红素边缘的正电性表面，其用作与氧化还原配偶体的对接位点。用LmCytc和LmP进行的动力学测定表明，LmCytc是比马心细胞色素c更好的LmP底物。此外，与充分研究的酵母系统不同，该反应遵循经典的Michaelis-Menten动力学，并且对增加的离子强度敏感。使用酵母共晶体作为对照，使用Rosetta进行蛋白质-蛋白质对接以开发LmP和LmCytc结合的模型。这些结果表明，LmP的生物学功能是作为细胞色素c过氧化物酶。
Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities. Our previous results illustrated that LmP has much higher activity against horse heart cytochrome c than ascorbate suggesting that cytochrome c may be the biologically important substrate. In order to elucidate the biological function of LmP, we have recombinantly expressed, purified and determined the 2.08Å crystal structure of Leishmania major cytochrome c (LmCytc). Like other cytochromes c LmCytc has an electropositive surface surrounding the exposed heme edge that serves as the docking site with redox partners. Kinetic assays performed with LmCytc and LmP show that LmCytc is a much better substrate for LmP than horse heart cytochrome c. Furthermore, unlike the well-studied yeast system, the reaction follows classic Michaelis-Menten kinetics and is sensitive to increasing ionic strength. Using the yeast co-crystal as a control, protein-protein docking was performed using Rosetta to develop a model for the binding of LmP and LmCytc. These results suggest that the biological function of LmP is to act as a cytochrome c peroxidase.
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