Small-volume potentiometric titrations: EPR investigations of Fe-S cluster N2 in mitochondrial complex I

J Inorg Biochem. 2016 Sep:162:201-206. doi: 10.1016/j.jinorgbio.2016.04.025. Epub 2016 Apr 20.

Abstract

EPR-based potentiometric titrations are a well-established method for determining the reduction potentials of cofactors in large and complex proteins with at least one EPR-active state. However, such titrations require large amounts of protein. Here, we report a new method that requires an order of magnitude less protein than previously described methods, and that provides EPR samples suitable for measurements at both X- and Q-band microwave frequencies. We demonstrate our method by determining the reduction potential of the terminal [4Fe-4S] cluster (N2) in the intramolecular electron-transfer relay in mammalian respiratory complex I. The value determined by our method, Em7=-158mV, is precise, reproducible, and consistent with previously reported values. Our small-volume potentiometric titration method will facilitate detailed investigations of EPR-active centres in non-abundant and refractory proteins that can only be prepared in small quantities.

Keywords: Electron paramagnetic resonance; Iron-sulfur clusters; NADH:ubiquinone oxidoreductase; Redox titrations.

MeSH terms

  • Animals
  • Catalytic Domain
  • Cattle
  • Electron Spin Resonance Spectroscopy
  • Electron Transport
  • Electron Transport Complex I / chemistry*
  • Electrons*
  • Iron / chemistry*
  • Mitochondria / chemistry*
  • Mitochondria / enzymology
  • Oxidation-Reduction
  • Potentiometry / methods*
  • Reproducibility of Results
  • Sulfur / chemistry*

Substances

  • Sulfur
  • Iron
  • Electron Transport Complex I