Institute for Biochemistry, Redox Biochemistry, University of Cologne, Zuelpicher Str. 47a, 50674 Cologne, Germany.
VIB-VUB Center for Structural Biology, Pleinlaan 2, 1050 Brussels, Belgium; Jean Jeener NMR Centre, VUB, Pleinlaan 2, 1050 Brussels, Belgium.
J Mol Biol. 2021 Jul 23;433(15):167045. doi: 10.1016/j.jmb.2021.167045. Epub 2021 May 8.
Being essential for oxidative protein folding in the mitochondrial intermembrane space, the mitochondrial disulfide relay relies on the electron transfer (ET) from the sulfhydryl oxidase Erv1 to cytochrome c (Cc). Using solution NMR spectroscopy, we demonstrate that while the yeast Cc-Erv1 system is functionally active, no observable binding of the protein partners takes place. The transient interaction between Erv1 and Cc can be rationalized by molecular modeling, suggesting that a large surface area of Erv1 can sustain a fast ET to Cc via a collision-type mechanism, without the need for a canonical protein complex formation. We suggest that, by preventing the direct ET to molecular oxygen (O), the collision-type Cc-Erv1 interaction plays a role in protecting the organism against reactive oxygen species.
作为线粒体膜间隙氧化蛋白折叠所必需的，线粒体二硫键中继依赖于电子转移（ET）从巯基氧化酶 Erv1 到细胞色素 c（Cc）。使用溶液 NMR 光谱，我们证明了虽然酵母 Cc-Erv1 系统具有功能活性，但没有观察到蛋白质伴侣之间的可检测结合。Erv1 和 Cc 之间的瞬时相互作用可以通过分子建模合理化，表明 Erv1 的大表面积可以通过碰撞型机制通过快速 ET 持续传递给 Cc，而不需要形成规范的蛋白质复合物。我们认为，通过防止直接 ET 到分子氧（O），碰撞型 Cc-Erv1 相互作用在保护生物体免受活性氧方面发挥作用。
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