PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE VANADIUM-DEPENDENT HALOPEROXIDASE FROM CORALLINA-OFFICINALIS

C RUSH, A WILLETTS, G DAVIES, Z DAUTER, H WATSON, J LITTLECHILD

Research output: Contribution to journalArticlepeer-review

Abstract

The vanadium-dependent haloperoxidase from the seaweed Corallina officinalis has been purified to homogeneity and crystallised, The protein is reported to be a hexamer of 12 x 64,000 Da, contains no haem, and is dependent on vanadium for activity. The crystals are grown from polyethylene glycol (PEG) 6,000 and 0.4 M potassium chloride, They are stable and diffract to better than 2 A resolution, They are of a cubic space group I23 (or I2(1)3) with cell dimensions a = b = c = 310 Angstrom.

Original languageEnglish
Pages (from-to)244-246
Number of pages3
JournalFEBS Letters
Volume359
Issue number2-3
Publication statusPublished - 13 Feb 1995

Keywords

  • HALOPEROXIDASE
  • VANADIUM ENZYME
  • CRYSTAL
  • X-RAY DIFFRACTION
  • BIOTRANSFORMATION
  • ASCOPHYLLUM-NODOSUM
  • REACTION-MECHANISM
  • BROMOPEROXIDASE
  • CHLOROPEROXIDASE
  • PILULIFERA
  • PEROXIDASE
  • ENZYME

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