Biosynthesis of coenzyme F430 in methanogenic bacteria. Identification of 15,17(3)-seco-F430-17(3)-acid as an intermediate

Eur J Biochem. 1987 Dec 30;170(1-2):459-67. doi: 10.1111/j.1432-1033.1987.tb13722.x.

Abstract

Coenzyme F430 is a hydroporphinoid nickel complex present in all methanogenic bacteria. It is part of the enzyme system which catalyzes methane formation from methyl-coenzyme M. We describe here that under certain conditions a second nickel porphinoid accumulates in methanogenic bacteria. The compound was identified at 15,17(3)-seco-F430-17(3)-acid. The structural assignment rests on 14C-labelling experiments, fast-atom-bombardment mass spectra, 1H-NMR spectra of the corresponding hexamethyl ester, and ultraviolet/visible spectral comparison with model compounds. In cell extracts and in intact cells of methanogenic bacteria, 15,17(3)-seco-F430-17(3)-acid was converted to F430. These findings indicate that the new nickel-containing porphinoid is an intermediate in the biosynthesis of coenzyme F430.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Coenzymes / biosynthesis*
  • Euryarchaeota / growth & development
  • Euryarchaeota / metabolism*
  • Magnetic Resonance Spectroscopy
  • Metalloporphyrins*
  • Metalloproteins / biosynthesis*
  • Metalloproteins / isolation & purification
  • Nickel / biosynthesis*
  • Nickel / isolation & purification
  • Nickel / metabolism*
  • Species Specificity
  • Spectrophotometry

Substances

  • Coenzymes
  • Metalloporphyrins
  • Metalloproteins
  • factor F430
  • Nickel