Seasonal changes in bromoperoxidase activity in coralline algae (Coral
linaceae) are responsible for the production of volatile halogenated c
ompounds. SDS-polyacrylamide gel electrophoresis (PAGE) of a crude pro
tein extract showed that the concentration of this enzyme was almost c
onstant throughout the year. Therefore, the enzyme activity in vivo ch
anged seasonally due to a structural alteration. To elucidate this, th
e metal content of this enzyme at different states of activity was mea
sured. The results revealed that the enzyme activity is controlled by
the incorporation of vanadate ions, less than 1.2 mol mol enzyme(-1),
in the active site of the enzyme.