Aerobic damage to [FeFe]-hydrogenases: activation barriers for the chemical attachment of O2.
Aerobic damage to [FeFe]-hydrogenases: activation barriers for the chemical attachment of O2.
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DOI：
10.1002/anie.201400534
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发表时间：
2014-04-14
影响因子：
16.6
通讯作者：
Blumberger, Jochen
中科院分区：
文献类型：
--
作者：
Kubas, Adam;De Sancho, David;Best, Robert B.;Blumberger, Jochen
[FeFe]-氢化酶是最好的天然产氢酶，但其生物技术开发因其极端的氧敏感性而受到阻碍。通过使用重新参数化的范围分离密度泛函来研究 O2 化学附着到酶活性位点的自由能分布，以重现高水平的从头计算数据。双铁活性位点和 O2 之间形成化学键时获得了 13kcalmol−1 的活化自由能势垒，该值与实验失活率非常吻合。氧结合可以被视为内球电子转移过程，该过程受到与近端立方烷簇和蛋白质环境的库仑相互作用的强烈影响。讨论了这些结果对未来旨在提高这种酶的氧耐受性的突变研究的影响。
[FeFe]-hydrogenases are the best natural hydrogen-producing enzymes but their biotechnological exploitation is hampered by their extreme oxygen sensitivity. The free energy profile for the chemical attachment of O2 to the enzyme active site was investigated by using a range-separated density functional re-parametrized to reproduce high-level ab initio data. An activation free-energy barrier of 13 kcal mol−1 was obtained for chemical bond formation between the di-iron active site and O2, a value in good agreement with experimental inactivation rates. The oxygen binding can be viewed as an inner-sphere electron-transfer process that is strongly influenced by Coulombic interactions with the proximal cubane cluster and the protein environment. The implications of these results for future mutation studies with the aim of increasing the oxygen tolerance of this enzyme are discussed.
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