Regulation of the redox metabolome and thiol proteome by hydrogen sulfide.

Regulation of the redox metabolome and thiol proteome by hydrogen sulfide.
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硫化氢对氧化还原代谢组和硫醇蛋白质组的调节。

DOI:
10.1080/10409238.2021.1893641
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发表时间:
2021-06
影响因子:
6.5
通讯作者:
Banerjee R
Banerjee R
中科院分区:
生物学2区
文献类型:
--
作者:
Kumar R;Banerjee R

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活性氧的过量产生和抗氧化防御的受损扰乱了细胞内氧化还原稳态,并与无数的人类疾病以及衰老的自然过程有关。硫化氢(H2S)是由从细菌到人类的各种生物合成的,影响着广泛的生理功能。H2S发挥其细胞作用的一个备受推崇的分子机制是通过巯基氧化还原蛋白质组的翻译后修饰,将半胱氨酸巯基转化为过硫化物,这一过程被称为蛋白质过硫化物。这种修饰在特定信号传递途径中的生理相关性仍有待严格确立,而蛋白质过硫化对半胱氨酸蛋白质组超氧化的一般保护作用得到了更好的支持。H2S调节氧化还原稳态的第二种机制是通过重塑氧化还原代谢组,以电子传递链为目标,扰乱主要氧化还原节点,即CoQ/CoQH2、NAD+/NADH和FAD/FADH2。h2s诱导的氧化还原变化引起的代谢变化从线粒体扇形向其他区室扩散。在这篇综述中,我们讨论了最近的研究进展,阐明H2S及其氧化产物在氧化还原稳态中的作用及其在保护硫醇蛋白质组中的作用。
Overproduction of reactive oxygen species and compromised antioxidant defenses perturb intracellular redox homeostasis and is associated with a myriad of human diseases as well as with the natural process of aging. Hydrogen sulfide (H2S), which is biosynthesized by organisms ranging from bacteria to man, influences a broad range of physiological functions. A highly touted molecular mechanism by which H2S exerts its cellular effects is via post-translational modification of the thiol redox proteome, converting cysteine thiols to persulfides, in a process referred to as protein persulfidation. The physiological relevance of this modification in the context of specific signal transmission pathways remains to be rigorously established, while a general protective role for protein persulfidation against hyper-oxidation of the cysteine proteome is better supported. A second mechanism by which H2S modulates redox homeostasis is via remodeling the redox metabolome, targeting the electron transfer chain and perturbing the major redox nodes i.e., CoQ/CoQH2, NAD+/NADH and FAD/FADH2. The metabolic changes that result from H2S-induced redox changes fan out from the mitochondrion to other compartments. In this review, we discuss recent developments in elucidating the roles of H2S and its oxidation products on redox homeostasis and its role in protecting the thiol proteome.
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