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首页> 外文期刊>Biochemistry >Binding of nucleotides by the mitochondrial ADP/ATP carrier as studied by 1H nuclear magnetic resonance spectroscopy.
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Binding of nucleotides by the mitochondrial ADP/ATP carrier as studied by 1H nuclear magnetic resonance spectroscopy.

机译：通过1H核磁共振波谱研究，线粒体ADP / ATP载体与核苷酸的结合。

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摘要

Nucleotide binding to the cytosolic binding site of the mitochondrial ADP/ATP carrier (AAC) was studied by 1H-nuclear magnetic resonance spectroscopy. Binding (as opposed to translocation) could be identified as a result of the rapid ligand on/off kinetics, using the cytosolic side specific inhibitor carboxyatractyloside (CAT) for the distinction from nonspecific interactions. The off rate constant of the nonhydrolyzable ATP analogue AMP-PCP was more than 3 orders of magnitude larger than the transport rate. The nucleotides adopt an anti conformation in the carrier binding site as shown by measurements of the transferred nuclear overhauser effect (TRNOE). A thermal transition around 14 degreesC that had been previously detected in transport studies [Klingenberg, M., Grebe, K., and Appel, M. (1982) Eur. J. Biochem. 126, 263-269] was reflected by the inhibitor sensitive line broadening, indicating that this transition also affects nucleotide binding. Nucleotide monophosphates were employed to study the relation between nucleotide structure and affinity, using selective excitation, sample spinning with digital suppression of spinning sidebands, and line shape simulation. The binding of purines depends on the distribution of the electrical potential and on the position of ring substituents, while pyrimidines are barely recognized at all by the AAC. It is also shown that the photocleavable "caged" derivatives are more tightly bound than the original nucleotides. A two step model of carrier catalysis will be discussed on the basis of these results.
机译：通过1H核磁共振波谱研究了核苷酸与线粒体ADP / ATP载体（AAC）胞质结合位点的结合。结合（相对于易位）可以通过快速的配体开/关动力学来鉴定，使用胞质侧特异性抑制剂羧白术苷（CAT）与非特异性相互作用进行区分。不可水解ATP类似物AMP-PCP的解离速率常数比传输速率大3个数量级。核苷酸在载体结合位点采取反构象，如对转移的核过度消耗效应（TRNOE）的测量所示。以前在运输研究中已经检测到大约14摄氏度的热转变[Klingenberg，M.，Grebe，K.和Appel，M.（1982）Eur。 J.生物化学。 [126，263-269]由抑制剂敏感线加宽反映出来，表明这种转变也影响核苷酸结合。核苷酸一磷酸被用于研究核苷酸结构和亲和力之间的关系，使用选择性激发，样品纺丝和数字抑制纺丝边带以及线形模拟。嘌呤的结合取决于电势的分布和环取代基的位置，而嘧啶几乎不能被AAC识别。还显示出光可裂解的“笼状”衍生物比原始核苷酸更紧密地结合。基于这些结果，将讨论载体催化的两步模型。

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