How are cytochrome b561 electron currents controlled by membrane voltage and substrate availability?

Antioxid Redox Signal. 2014 Jul 20;21(3):384-91. doi: 10.1089/ars.2013.5809. Epub 2014 Feb 20.

Abstract

Direct recordings of electron currents mediated by cytochromes b561 (CYB561) are not available yet, despite the importance of these proteins in a variety of physiological functions, including neurotransmitter synthesis and dietary iron uptake. Here, we used the two-electrode voltage-clamp technique applied to Xenopus oocytes to demonstrate, for the first time, the generation of electron currents by a Drosophila member of the CYB561 superfamily named stromal cell-derived receptor 2 (SDR2). This experimental method, along with the theoretical development of a three-state kinetic model, supports the hypothesis that electron donor/acceptor concentrations and transmembrane voltage mutually control SDR2-mediated electron transport activity in a complex but predictable manner.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cytochrome b Group / chemistry*
  • Cytochrome b Group / metabolism
  • Drosophila / metabolism
  • Electrons*
  • Kinetics
  • Membranes / chemistry
  • Oxidation-Reduction*
  • Patch-Clamp Techniques
  • Receptors, Cell Surface / chemistry*
  • Receptors, Cell Surface / metabolism
  • Substrate Specificity
  • Xenopus laevis

Substances

  • Cytochrome b Group
  • Receptors, Cell Surface
  • cytochrome b561