Heme Is Not Required for Aquifex aeolicus Cytochrome c555 Polypeptide Folding
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概要
- 論文の詳細を見る
In cytochrome c, it has been supposed that heme must bind to the apo polypeptide for structure formation. We constructed a C12A/C15A variant of hyperthermophilic Aquifex aeolicus cytochrome c555 (AA c555) in which the covalently heme-binding Cys residues were replaced by Ala, and characterized its molecular features. The apo C12A/C15A variant had almost the same helical content as holo AA c555, and spontaneously incorporated heme in vitro with no helical content change. These results suggest that the apo AA c555 polypeptide is intrinsically structured without heme binding, this being the first case of a cytochrome c polypeptide. This finding provides a new suggestion as to cytochrome c formation, that heme is not necessarily required for cytochrome c polypeptide folding.
著者
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Yamanaka Masaru
Graduate School of Biosphere Science, Hiroshima University, CREST of Japan Science and Technology Co
-
Mita Hajime
Department of Chemistry, University of Tsukuba
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Yamamoto Yasuhiko
Department of Chemistry, University of Tsukuba
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SAMBONGI Yoshihiro
Graduate School of Biosphere Science, Hiroshima University, CREST of Japan Science and Technology Co
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