Topography of human cytochrome b5/cytochrome b5 reductase interacting domain and redox alterations upon complex formation

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Cytochrome b5 is the main electron acceptor of cytochrome b5 reductase. The interacting domain between both human proteins has been unidentified up to date and very little is known about its redox properties modulation upon complex formation. In this article, we characterized the protein/protein interacting interface by solution NMR and molecular docking. In addition, upon complex formation, we measured an increase of cytochrome b5 reductase flavin autofluorescence that was dependent upon the presence of cytochrome b5. Data analysis of these results allowed us to calculate a dissociation constant value between proteins of 0.5 ± 0.1 μM and a 1:1 stoichiometry for the complex formation. In addition, a 30 mV negative shift of cytochrome b5 reductase redox potential in presence of cytochrome b5 was also measured. These experiments suggest that the FAD group of cytochrome b5 reductase increase its solvent exposition upon complex formation promoting an efficient electron transfer between the proteins.

Original languageEnglish
Pages (from-to)78-87
Number of pages10
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1859
Issue number2
DOIs
Publication statusPublished - Feb 2018

Keywords

  • Autofluorescence
  • Cytochrome b
  • Cytochrome b reductase
  • Dissociation constant
  • Redox potential

Fingerprint Dive into the research topics of 'Topography of human cytochrome b<sub>5</sub>/cytochrome b<sub>5</sub> reductase interacting domain and redox alterations upon complex formation'. Together they form a unique fingerprint.

  • Cite this