Expression and characterization of recombinant human cytochrome c in E. coli

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)

Abstract

Cytochrome c is a heme protein involved in electron transfer, cell apoptosis, and diseases associated with oxidative stress. Here we expressed human cytochrome c in E. coli and purified it to homogeneity with a yield of 10-15 mg/L. The redox potential of recombinant human cytochrome c was 0.246 V which was measured by cyclic voltammetry. This is similar to that of horse cytochrome c with a value of 0.249 V. The sequential assignment and structural analysis of recombinant human ferrocytochrome c were obtained using multidimensional NMR spectroscopy. On the basis of our NMR studies, the recombinant human cytochrome c produced in E. coli exhibits the same tertiary fold as horse cytochrome c. These results provide evidence that human cytochrome c expressed in E. coli possesses a similar function and structure to that of the horse protein. It is known that cytochrome c plays a role in many human diseases. This study serves as the basis for gaining insight into human diseases by exploring structure and function relationships of cytochrome c to its interacting proteins.

Original languageEnglish
Pages (from-to)423-431
Number of pages9
JournalJournal of Bioenergetics and Biomembranes
Volume34
Issue number6
DOIs
Publication statusPublished - 2002 Dec 1

All Science Journal Classification (ASJC) codes

  • Physiology
  • Cell Biology

Fingerprint Dive into the research topics of 'Expression and characterization of recombinant human cytochrome c in E. coli'. Together they form a unique fingerprint.

Cite this