A simple complex on the verge of breakdown: isolation of the elusive cyanoformate ion

Science. 2014 Apr 4;344(6179):75-8. doi: 10.1126/science.1250808.

Abstract

Why does cyanide not react destructively with the proximal iron center at the active site of 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase, an enzyme central to the biosynthesis of ethylene in plants? It has long been postulated that the cyanoformate anion, [NCCO2](-), forms and then decomposes to carbon dioxide and cyanide during this process. We have now isolated and crystallographically characterized this elusive anion as its tetraphenylphosphonium salt. Theoretical calculations show that cyanoformate has a very weak C-C bond and that it is thermodynamically stable only in low dielectric media. Solution stability studies have substantiated the latter result. We propose that cyanoformate shuttles the potentially toxic cyanide away from the low dielectric active site of ACC oxidase before breaking down in the higher dielectric medium of the cell.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Oxidoreductases / chemistry
  • Amino Acid Oxidoreductases / metabolism*
  • Carbon Dioxide / chemistry
  • Catalytic Domain
  • Crystallization
  • Cyanides / chemistry
  • Ethylenes / metabolism
  • Formates / chemistry
  • Formates / isolation & purification*
  • Magnetic Resonance Spectroscopy
  • Molecular Structure
  • Nitriles / chemistry
  • Nitriles / isolation & purification*
  • Thermodynamics
  • X-Ray Diffraction

Substances

  • Cyanides
  • Ethylenes
  • Formates
  • Nitriles
  • Carbon Dioxide
  • ethylene
  • Amino Acid Oxidoreductases
  • 1-aminocyclopropane-1-carboxylic acid oxidase