1 Institute for Molecular Bioscience, The University of Queensland , St. Lucia, Australia .
Antioxid Redox Signal. 2013 Dec 1;19(16):1976-80. doi: 10.1089/ars.2013.5365. Epub 2013 Jun 19.
Vicinal disulfide bridges, in which a disulfide bond is formed between adjacent cysteine residues, constitute an unusual but expanding class of potential allosteric disulfides. Although vicinal disulfide rings (VDRs) are relatively uncommon, they have proven to be functionally critical in almost all proteins in which they have been discovered. However, it has proved difficult to test whether these sterically constrained disulfides participate in functionally important redox transformations. We demonstrate that chemical replacement of VDRs with dicarba or diselenide bridges can be used to assess whether VDRs function as allosteric disulfides. Our approach leads to the hypothesis that not all VDRs participate in functionally important redox reactions.
毗邻二硫键，其中一个二硫键在相邻的半胱氨酸残基之间形成，构成了一类不常见但不断扩大的潜在别构二硫键。虽然毗邻二硫环（VDR）相对较少，但它们已被证明在几乎所有已发现的蛋白质中都是功能关键的。然而，事实证明，很难测试这些空间受限的二硫键是否参与功能重要的氧化还原转化。我们证明，用二碳或二硒桥替代 VDR 可以用于评估 VDR 是否作为别构二硫键发挥作用。我们的方法导致了这样的假设，即并非所有的 VDR 都参与功能重要的氧化还原反应。
