The reactions of hydropersulfides (RSSH) with myoglobin
The reactions of hydropersulfides (RSSH) with myoglobin
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DOI：
10.1016/j.abb.2020.108391
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发表时间：
2020-07-15
影响因子：
3.9
通讯作者：
Fukuto, Jon M.
中科院分区：
文献类型：
--
作者：
Alvarez, Lucia;Vega, Valeria Suarez;Fukuto, Jon M.
据报道，过硫氢化物是良好的生物还原剂，上级于硫醇，类似于硒醇。因此，它们先前已经显示在很少或没有观察到从相应硫醇的还原的条件下将金属蛋白如铁肌红蛋白和铁细胞色素c还原成它们的亚铁形式。毫不奇怪，在有氧条件下铁肌红蛋白还原为亚铁肌红蛋白导致氧合肌红蛋白（双氧结合亚铁肌红蛋白）的产生。先前的研究表明，氧合肌红蛋白还可以与羟胺和抗坏血酸盐等高度还原物质一起充当氧化剂。考虑到氢过硫化物的还原性质，它们也可能与氧合肌红蛋白发生类似于羟胺或抗坏血酸盐的反应。在本文中，检查了该反应，并且确实发现过硫酸氢盐与氧合肌红蛋白反应，类似于其他还原物质，导致短暂的铁肌红蛋白，其也被过硫酸氢盐快速还原为亚铁形式。
Hydropersulfides are reported to be good biological reductants, superior to thiols and akin to selenols. As such, they have been previously shown to reduce metalloproteins such as ferric myoglobin and ferric cytochrome c to their ferrous forms under conditions where little or no reduction from corresponding thiols is observed. Not surprisingly, the reduction of ferric myoglobin to ferrous myoglobin under aerobic conditions results in the generation of oxymyoglobin (dioxygen bound ferrous myoglobin). Previous studies have demonstrated that oxymyoglobin can also act as an oxidant with highly reducing species such as hydroxylamine and ascorbate. Considering the reducing properties of hydropersulfides, it is possible that they can also react with oxymyoglobin similarly to hydroxylamine or ascorbate. Herein, this reaction is examined and indeed hydropersulfides are found to react with oxymyoglobin similarly to other reducing species leading to a fleeting ferric myoglobin which is rapidly reduced to the ferrous form also by hydropersulfide.