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Article: Data on biochemistry reported by researchers at Hiroshima University.
- Article from:
- Chemicals & Chemistry
- Article date:
- November 13, 2009
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According to recent research from Japan, "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 c(555) (AA c(555)) 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 c(555), and spontaneously incorporated heme in vitro with no helical content change. These results suggest that the apo AA c(555) polypeptide is intrinsically structured without heme binding, this being the first case of a ...
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... ... wrote T. Tokunaga and colleagues, Hiroshima University. The researchers concluded ... obtained by contacting M. Esaka, Hiroshima University, Graduate School Biosphere Science ... Sciences, Physiology, Botany, Hiroshima University. This article was prepared by Life ...
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