Magnetic Resonance Center CERM, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.
Consorzio Interuniversitario Risonanze Magnetiche di Metalloproteine (CIRMMP), Via L. Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.
Angew Chem Int Ed Engl. 2021 Jun 25;60(27):14841-14845. doi: 10.1002/anie.202102910. Epub 2021 May 24.
Human anamorsin is an iron-sulfur (Fe-S)-cluster-binding protein acting as an electron donor in the early steps of cytosolic iron-sulfur protein biogenesis. Human anamorsin belongs to the eukaryotic CIAPIN1 protein family and contains two highly conserved cysteine-rich motifs, each binding an Fe-S cluster. In vitro works by various groups have provided rather controversial results for the type of Fe-S clusters bound to the CIAPIN1 proteins. In order to unravel the knot on this topic, we used an in cellulo approach combining Mössbauer and EPR spectroscopies to characterize the iron-sulfur-cluster-bound form of human anamorsin. We found that the protein binds two [2Fe-2S] clusters at both its cysteine-rich motifs.
人源 anamorsin 是一种铁硫簇(Fe-S)结合蛋白,在细胞质铁硫蛋白生物发生的早期步骤中作为电子供体发挥作用。人源 anamorsin 属于真核 CIAPIN1 蛋白家族,含有两个高度保守的富含半胱氨酸的基序,每个基序都结合一个 Fe-S 簇。不同研究小组的体外研究结果对结合到 CIAPIN1 蛋白上的 Fe-S 簇的类型提供了相当有争议的结果。为了解开这个谜团,我们使用体内方法结合 Mössbauer 和 EPR 光谱学来表征人源 anamorsin 的铁硫簇结合形式。我们发现该蛋白在其两个富含半胱氨酸的基序处均结合两个 [2Fe-2S] 簇。