High stability of apo-cytochrome c' from thermophilic Hydrogenophilus thermoluteolus

Biosci Biotechnol Biochem. 2014;78(7):1191-4. doi: 10.1080/09168451.2014.912120. Epub 2014 May 28.

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.

Keywords: apo-cytochrome c’; circular dichroism; helix content; stability; thermophile.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Apoenzymes / chemistry
  • Cytochromes c / chemistry*
  • Enzyme Stability
  • Hydrogenophilaceae / enzymology*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary

Substances

  • Apoenzymes
  • Cytochromes c