Purification and characterization of two proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris: rubrerythrin and a new, highly active, enzyme

Biochem Biophys Res Commun. 1990 Aug 31;171(1):313-8. doi: 10.1016/0006-291x(90)91394-8.

Abstract

The inorganic pyrophosphatase activity of a soluble extract from the strict anaerobe, sulfate-reducing, Desulfovibrio vulgaris, is readily resolved into two peaks. After purification, two active proteins with very dissimilar properties are obtained. One is the non-heme iron-containing rubrerythrin, with a specific activity of 350 pyrophosphate hydrolyzed, min-1, mg protein-1. The other, a protein of Mr = 39,000, with a specific activity of 12,000.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Bacterial Proteins / isolation & purification*
  • Bacterial Proteins / metabolism
  • Chromatography
  • Desulfovibrio / enzymology*
  • Ferredoxins / isolation & purification*
  • Ferredoxins / metabolism
  • Hemerythrin
  • Molecular Sequence Data
  • Pyrophosphatases / isolation & purification*
  • Rubredoxins
  • Solubility
  • Spectrophotometry, Ultraviolet

Substances

  • Amino Acids
  • Bacterial Proteins
  • Ferredoxins
  • Hemerythrin
  • Rubredoxins
  • rubrerythrins
  • Pyrophosphatases