Hyafil F, Bernassau J M
Eur J Biochem. 1978 Apr 17;85(2):419-22. doi: 10.1111/j.1432-1033.1978.tb12254.x.
Enhancement of the nuclear relaxation rates by manganese has been used to derive manganese--purine-ring distances in the activation site of methionyl-tRNA synthetase. This is possible with the help of an abortive complex between the enzyme, methionine, adenosine, pyrophosphate and manganese which simulates an intermediate species of the activation reaction. It is found that the distances between the manganese ion and the purine ring are too high (greater than 0.8 nm) to allow interaction between them. Thus, metal-purine interaction is involved neither in the catalytic mechanism nor in the stabilization of abortive synergistic complexes [S. Blanquet, G. Fayat and J. P. Waller (1975) J. Mol. Biol. 94, 1-15].
通过锰增强核弛豫速率已被用于推导甲硫氨酰 - tRNA合成酶活性位点中锰与嘌呤环之间的距离。这借助于酶、甲硫氨酸、腺苷、焦磷酸和锰之间的一种无效复合物得以实现，该复合物模拟了活化反应的一个中间物种。研究发现，锰离子与嘌呤环之间的距离过大（大于0.8纳米），无法使它们之间发生相互作用。因此，金属 - 嘌呤相互作用既不参与催化机制，也不参与无效协同复合物的稳定作用 [S. 布兰凯、G. 法亚特和J. P. 沃勒（1975年）《分子生物学杂志》94卷，第1 - 15页] 。
