Vanadate activation of bromoperoxidase from Corallina officinalis

Hong Yu, James Whittaker

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

A nonheme bromoperoxidase has been purified to homogeneity from the red seaweed Corallina officinalis. Like the corresponding enzyme previously reported from C. pilulifera, this bromoperoxidase contains a significant amount of nonheme iron. However, it is vanadate ion and not iron that activates the enzyme, and maximal activity is achieved with stoichiometric vanadium incorporation. The absence of competition between vanadium and iron suggests that they occupy distinct binding sites in the protein. A correlation between vanadium content and catalytic activity indicates that less than 12 percent of the maximal activity of the enzyme can be derived from metals other than vanadium.

Original languageEnglish (US)
Pages (from-to)87-92
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume160
Issue number1
DOIs
StatePublished - Apr 14 1989
Externally publishedYes

Fingerprint

Vanadium
Vanadates
Chemical activation
Iron
Enzymes
Seaweed
Catalyst activity
Metals
Binding Sites
Ions
bromide peroxidase
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Vanadate activation of bromoperoxidase from Corallina officinalis. / Yu, Hong; Whittaker, James.

In: Biochemical and Biophysical Research Communications, Vol. 160, No. 1, 14.04.1989, p. 87-92.

Research output: Contribution to journalArticle

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