Barrier Compression Enhances an Enzymatic Hydrogen-Transfer Reaction
Barrier Compression Enhances an Enzymatic Hydrogen-Transfer Reaction
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DOI：
10.1002/anie.200805502
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发表时间：
2009-01-01
影响因子：
16.6
通讯作者：
Scrutton, Nigel S.
中科院分区：
文献类型：
--
作者：
Hay, Sam;Pudney, Christopher R.;Scrutton, Nigel S.
施加挤压：静水压力会导致吗啡酮还原酶和 NADH4 的二元复合物中的电荷转移键缩短（见图）。分子动力学模拟表明，压力通过限制活性位点内黄素单核苷酸和 NADH 可用的构象空间来减少平均反应势垒宽度。表观催化速率随压力增加而增加。
Putting the squeeze on: Hydrostatic pressure causes a shortening of the charge‐transfer bond in the binary complex of morphinone reductase and NADH4(see diagram). Molecular dynamics simulations suggest that pressure reduces the average reaction barrier width by restricting the conformational space available to the flavin mononucleotide and NADH within the active site. The apparent rate of catalysis increases with pressure.