期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 60, 期 27, 页码 14841-14845出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202102910
关键词
anamorsin; in cellulo EPR spectroscopy; in cellulo Mcssbauer spectroscopy; iron-sulfur clusters; metalloproteins
资金
- Instruct-ERIC, an ESFRI Landmark Research Infrastructure
- Timb3 - Horizon 2020 research and innovation programme of the European Commission [810856]
- Italian Ministry for University and Research (FOE funding)
- COST (European Co-operation in Science and Technology) [CA15133]
- Labex ARCANE
- Labex CBH-EUR-GS [ANR-17-EURE-0003]
Studies have shown that human anamorsin protein binds two [2Fe-2S] clusters at both its cysteine-rich motifs.
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 Mossbauer 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.
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