title: High stability of apo-cytochrome c' from thermophilic Hydrogenophilus thermoluteolus.
abstract: Apo-cytochomes c without heme are usually unstructured. Here we showed that apo-form of thermophilic Hydrogenophilus thermoluteolus cytochrome c' (PHCP) was a monomeric protein with high helix content. Apo-PHCP was thermally stable, possibly due to the hydrophobic residues and ion pairs. PHCP is the first example of a structured apo-cytochrome c', which will expand our view of hemoprotein structure formation.
authors.affiliation: a Graduate School of Biosphere Science , Hiroshima University , Higashi-Hiroshima , Japan.
authors.forename: Sotaro
authors.initials: S
authors.lastname: Fujii
authors.forename: Misa
authors.initials: M
authors.lastname: Masanari
authors.forename: Masaru
authors.initials: M
authors.lastname: Yamanaka
authors.forename: Satoshi
authors.initials: S
authors.lastname: Wakai
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Sambongi
mesh_terms: D000595:Amino Acid Sequence; D001051:Apoenzymes / Q000737:chemistry; D045304:Cytochromes c / Q000737:chemistry*; D004795:Enzyme Stability; D043363:Hydrogenophilaceae / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary
chemical_list: D001051:Apoenzymes; D045304:Cytochromes c
keywords: apo-cytochrome c’; circular dichroism; helix content; stability; thermophile