期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 53, 期 51, 页码 14060-14063出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201408105
关键词
force spectroscopy; iron priming; metalloproteins; protein folding; single-molecule studies
资金
- Natural Sciences and Engineering Research Council of Canada
- Canada Foundation for Innovation
- Canada Research Chairs program
- Tianjin University
In metalloproteins, metal centers serve as active sites for a range of functional purposes and as important structural elements to facilitate protein folding and assembly. It is challenging to observe the reversible unfolding and refolding of metalloproteins because of a loss or decomposition of the metal center. Here, the reversible unfolding-refolding of the iron-sulfur protein rubredoxin was observed directly using single-molecule force spectroscopy. The results demonstrate that the iron can remain attached to the CXXC motif when rubredoxin is unfolded. Upon relaxation, the unfolded rubredoxin can refold into its native holo state with the reconstituted FeS4 center. The possible loss of iron from the unfolded protein prevents rubredoxin from refolding into its native holo state. These results demonstrated that unfolding of rubredoxin is reversible, as long as the iron remains attached, and provide experimental evidence for the iron-priming mechanism for the folding of rubredoxin.
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