Revealing the Membrane-Bound Catalytic Oxidation of NADH by the Drug Target Type-II NADH Dehydrogenase

Biochemistry. 2019 Oct 22;58(42):4272-4275. doi: 10.1021/acs.biochem.9b00752. Epub 2019 Oct 10.

Abstract

Type-II NADH:quinone oxidoreductases (NDH-2s) are an important element of microbial pathogen electron transport chains and an attractive drug target. Despite being widely studied, its mechanism and catalysis are still poorly understood in a hydrophobic membrane environment. A recent report for the Escherichia coli NDH-2 showed NADH oxidation in a solution-based assay but apparently showed the reverse reaction in electrochemical studies, calling into question the validity of the electrochemical approach. Here we report electrochemical catalysis in the well-studied NDH-2 from Caldalkalibacillus thermarum (CthNDH-2). In agreement with previous reports, we demonstrated CthNDH-2 NADH oxidation in a solution assay and electrochemical assays revealed a system artifact in the absence of quinone that was absent in a membrane system. However, in the presence of either immobilized quinone or mobile quinone in a membrane, NADH oxidation was observed as in solution-phase assays. This conclusively establishes surface-based electrochemistry as a viable approach for interrogating electron transfer chain drug targets.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillaceae / enzymology*
  • Benzoquinones / metabolism
  • Biocatalysis
  • Catalytic Domain
  • Dielectric Spectroscopy
  • Electrodes
  • Electron Transport
  • Electron Transport Chain Complex Proteins / metabolism*
  • Kinetics
  • Lipid Bilayers / metabolism
  • NAD / metabolism*
  • NADH Dehydrogenase / metabolism*
  • Vitamin K 3 / metabolism

Substances

  • Benzoquinones
  • Electron Transport Chain Complex Proteins
  • Lipid Bilayers
  • NAD
  • quinone
  • Vitamin K 3
  • NADH Dehydrogenase

Supplementary concepts

  • Caldalkalibacillus thermarum