Evidence for a Proton-Coupled Electron Transfer Mechanism in a Biomimetic System for Monoamine Oxidase B Catalysis

Chemistry. 2020 Jan 16;26(4):823-829. doi: 10.1002/chem.201904634. Epub 2020 Jan 7.

Abstract

Mechanistic studies with 5-ethyl-3-methyllumiflavinium (Fl+ ) perchlorate, a biomimetic model for flavoenzyme monoamine oxidase B (MAO-B) catalysis, and the tertiary, allyl amine 1-methyl-4-(1-methyl-1 H-pyrrol-2-yl)-1,2,3,6-tetrahydropyridine (MMTP) reveal that proton-coupled electron transfer (PCET) may be an important pathway for MAO catalysis. The first step involves a single-electron transfer (SET) leading to the free radicals Fl. and MMTP. , the latter produced by deprotonation of the initially formed and highly acidic MMTP.+ . Molecular oxygen (O2 ) is found to play a hitherto unrecognized role in the early steps of the oxidation. MMTP and several structurally similar tertiary amines are the only tertiary amines oxidized by MAO, and their structural/electronic properties provide the key to understanding this behavior. A general hypothesis about the role of SET in MAO catalysis, and the recognition that PCET occurs with appropriately substituted substrates is presented.

Keywords: MAO catalysis; deprotonation; proton-coupled electron transfer; radical cations; single-electron transfer.

MeSH terms

  • Amines / chemistry*
  • Biomimetics
  • Catalysis
  • Electron Transport
  • Free Radicals / chemistry
  • Free Radicals / metabolism*
  • Monoamine Oxidase / chemistry*
  • Oxidation-Reduction
  • Protons

Substances

  • Amines
  • Free Radicals
  • Protons
  • Monoamine Oxidase