High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor

Nurit Mirkin, Jean Jaconcic, Vivian Stojanoff, Abel Moreno

Research output: Contribution to journalArticlepeer-review

93 Scopus citations

Abstract

Cytochrome c is one of the most studied proteins probably due to its electron-transfer properties in aerobic and anaerobic respiration. Particularly, cytochrome c from bovine heart is a small protein, Mr 12,230 Da, globular (hydrodynamic diameter of 3.4 nm), soluble in different buffer solutions, and commercially available. Despite being a quite well-studied protein and relatively easy to manipulate from the biochemical and electrochemical viewpoint, its 3D structure has never been published. In this work, the purification, crystallization and 3D structure of one of the cytochrome c isoforms is presented to 1.5 Å resolution. It is also shown how the presence of isoforms made both the purification and crystallization steps difficult. Finally, a new approach for protein electrocrystallization and design of biosensors is presented.

Original languageEnglish
Pages (from-to)83-92
Number of pages10
JournalProteins: Structure, Function and Bioinformatics
Volume70
Issue number1
DOIs
StatePublished - Jan 2008
Externally publishedYes

Keywords

  • Atomic force microscopy
  • Cytochrome c from bovine heart mitochondria
  • Electrocrystallization
  • Gel acupuncture method
  • X-ray diffraction

Fingerprint

Dive into the research topics of 'High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor'. Together they form a unique fingerprint.

Cite this