Revisiting sulfur H-bonds in proteins: The example of peroxiredoxin AhpE.
Revisiting sulfur H-bonds in proteins: The example of peroxiredoxin AhpE.
复制标题
重新访问蛋白质中的硫H键：过氧蛋白AHPE的例子。
DOI：
10.1038/srep30369
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发表时间：
2016-07-29
影响因子：
4.6
通讯作者：
Messens J
中科院分区：
文献类型：
--
作者：
van Bergen LA;Alonso M;Palló A;Nilsson L;De Proft F;Messens J
In many established methods, identification of hydrogen bonds (H-bonds) is primarily based on pairwise comparison of distances between atoms. These methods often give rise to systematic errors when sulfur is involved. A more accurate method is the non-covalent interaction index, which determines the strength of the H-bonds based on the associated electron density and its gradient. We applied the NCI index on the active site of a single-cysteine peroxiredoxin. We found a different sulfur hydrogen-bonding network to that typically found by established methods, and we propose a more accurate equation for determining sulfur H-bonds based on geometrical criteria. This new algorithm will be implemented in the next release of the widely-used CHARMM program (version 41b), and will be particularly useful for analyzing water molecule-mediated H-bonds involving different atom types. Furthermore, based on the identification of the weakest sulfur-water H-bond, the location of hydrogen peroxide for the nucleophilic attack by the cysteine sulfur can be predicted. In general, current methods to determine H-bonds will need to be reevaluated, thereby leading to better understanding of the catalytic mechanisms in which sulfur chemistry is involved.
