由和离子结合诱导的细胞染色体c氧化酶的结构变化:ATR-FTIR研究
Amandine Maréchal1, Masayo Iwaki, Peter R Rich
1Glynn Laboratory of Bioenergetics, Institute of Structural and Molecular Biology, University College London, Gower Street, London, WC1E 6BT, United Kingdom. a.marechal@ucl.ac.uk
Journal of the American Chemical Society
|March 30, 2013
概括
(Na+) 和 (Ca2+) 离子与牛细胞染色体c氧化酶的结合方式不同,具有竞争性的结合性. 这些发现揭示了对这种关键酶的离子结合和潜在功能调节的洞察力.
科学领域:
- 生物化学 生物化学
- 生物物理学的生物物理.
- 频谱学是一种光谱学.
背景情况:
- 细胞染色体c氧化酶 (CcO) 是细胞呼吸中至关重要的酶.
- 了解阴离子结合对于阐明酶结构和功能至关重要.
研究的目的:
- 通过ATR-FTIR光谱学研究Na+和Ca2+离子与牛细胞染色体c氧化酶的结合.
- 为了比较由Na+和Ca2+结合在酶的不同氧化还原状态中引起的结构变化.
主要方法:
- 减弱的总反射里埃变换红外光谱学 (ATR-FTIR).
- 氧化和化物合 (混合价值) 形式的酶的研究.
- 确定分离常数和分析光谱变化.
主要成果:
- Na+和Ca2+离子诱导了不同的相互排斥的红外线结合光谱,证实了竞争性的结合.
- 确定了解离常数:Na+为1.2mM,Ca2+为11μM与氧化酶.
- Ca2+ 结合导致多结构和血红蛋白的显著变化,而 Na+ 结合导致较弱的变化.
结论:
- 阴离子结合诱导细胞染色体c氧化酶的差异性结构变化.
- Na+和Ca2+的结合可以调节酶的结构和潜在的催化功能.
- 在酵母CcO结合光谱中观察到的差异表明,物种之间离子结合部位的可访问性有所不同.
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