The sulfinic acid switch in proteins
The sulfinic acid switch in proteins
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DOI：
10.1039/b406180b
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发表时间：
2004-01-01
影响因子：
3.2
通讯作者：
Fry, FH
中科院分区：
文献类型：
--
作者：
Jacob, C;Holme, AL;Fry, FH
最近对肽和蛋白质中半胱氨酸残基氧化还原行为的研究极大地改变了我们对氨基酸在生物催化、细胞内氧化还原传感和细胞信号传导中作用的看法。例如，蛋白质中半胱氨酸亚磺酸的形成长期以来被视为不可逆的“过度氧化”过程，可能导致活性丧失，特别是在氧化应激条件下。去年，几个研究小组独立证明亚磺酸可以在体内还原为硫醇。一种具有亚磺酸还原酶活性的酶，称为硫氧还蛋白，已从酵母中分离出来，并且已在人类基因组中鉴定出编码人类类似物的基因。亚磺酸形成的可逆性为一系列尚未探索的氧化还原循环、细胞信号传导过程和还原机制打开了大门。这些基于半胱氨酸的氧化还原过程将引起化学家、生物化学家、生物学家和医学界的极大兴趣。
Recent studies on the redox behaviour of cysteine residues in peptides and proteins have dramatically changed our perspective of the amino acid's role in biocatalysis, intracellular redox sensing and cell signalling. Cysteine sulfinic acid formation in proteins, for example, has long been viewed as an irreversible 'overoxidation' process that might lead to loss of activity, especially under conditions of oxidative stress. Within the last year, several research groups have independently shown that sulfinic acids can be reduced to thiols in vivo. An enzyme with sulfinic acid reductase activity, called sulfiredoxin, has been isolated from yeast and a gene encoding a human analogue has been identified in the human genome. Reversibility of sulfinic acid formation opens the door to a range of yet unexplored redox cycles, cell signalling processes and reduction mechanisms. These cysteine-based redox processes will be of enormous interest to chemists, biochemists, biologists and the medical community alike.