Multiscale Modeling of the Active Site of [Fe] Hydrogenase: The H2 Binding Site in Open and Closed Protein Conformations

被引：16

作者：

Hedegard, Erik Donovan ^{[1
]}

Kongsted, Jacob ^{[1
]}

Ryde, Ulf ^{[2
]}

机构：

[1] Univ Southern Denmark, Dept Phys Chem & Pharm, DK-5230 Odense M, Denmark

[2] Lund Univ, Dept Theoret Chem, S-22100 Lund, Sweden

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2015年 / 54卷 / 21期

基金：

瑞典研究理事会;

关键词：

Fe] hydrogenase; hydrogen activation; molecular mechanics; multiscale modeling; quantum mechanics; FE-57; MOSSBAUER-SPECTROSCOPY; CLUSTER-FREE HYDROGENASE; CRYSTAL-STRUCTURE; GEOMETRY OPTIMIZATIONS; REACTION ENERGIES; FORCE-FIELD; ACTIVATION; COMPLEX; HMD; REVEALS;

D O I：

10.1002/anie.201501737

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A series of QM/MM optimizations of the full protein of [Fe] hydrogenase were performed. The FeGP cofactor has been optimized in the water-bound resting state (1), with a side-on bound dihydrogen (2), or as a hydride intermediate (3). For inclusion of H4MPT in the closed structure, advanced multiscale modeling appears to be necessary, especially to obtain reliable distances between CH-H4MPT+ and the dihydrogen (H-2) or hydride (H-) ligand in the FeGP cofactor. Inclusion of the full protein is further important for the relative energies of the two intermediates 2 and 3. We finally find that hydride transfer from 3 has a significantly higher barrier than found in previous studies neglecting the full protein environment.

引用

页码：6246 / 6250

页数：5

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