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A Brominating and Hydroxylating Peroxidase from the Red Alga Cystoclonium purpureum
Author(s) -
PEDERSÉN MARIANNE
Publication year - 1976
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1976.tb01864.x
Subject(s) - alcohol , chemistry , enzyme , peroxidase , bromide , formic acid , absorption (acoustics) , medicinal chemistry , nuclear chemistry , organic chemistry , physics , acoustics
A particulate enzyme displaying peroxidase activity has been extracted from the red alga Cystoclonium purpureum (Huds.) Batt. The enzyme preparation was shown to contain ferri‐protoporphyrin IX through its formation of formic acid hemochromogen with absorption maxima at 399, 402, 555 and 600 nm. The preparation catalyses the formation of 3‐bromo‐ p ‐hydroxybenzyl alcohol from p ‐hydroxybenzyl alcohol in the presence of H 2 O 2 and NaBr at pH = 5.4. The formation of 3‐bromo‐ p ‐hydroxybenzyl alcohol was measured by gas chromato‐graphy‐mass spectrometry. At pH = 6.7, 4,5‐di‐hydroxybenzyl alcohol was formed. Addition of homogentisic acid stimulated the formation of dihydroxybenzyl alcohol and suppressed the brominating reaction. Iodide inhibits the enzyme. The results are consistent with a two‐site model of the enzyme.