Reactions of Ferrous and Ferric Ions with Hydrogen Peroxide

The chemical oxidation of phenol and chlorophenols with hydrogen peroxide in the presence of soluble iron can be economically attractive at low oxidant consumption, leading then to intermediates that are more easily biodegradable. The homogeneous oxidation of phenol and chlorophenols in aqueous solutions with hydrogen peroxide is studied at oxidant : phenol ratio of about 4:1 and 16:1 (mol/mol) at various catalyst concentrations, at ambient temperature without pH control. Ferric chloride, ferric and ferrous sulphate and ferrous ammonium sulphate are used as oxidation catalysts. Ferric salts induce higher oxidation rates than ferrous ones and the nature of the anions present does not affect reaction rate. 4-Chlorophenol is found to be most resistant to oxidation and 2,4,6-Trichlorophenol is not attacked by hydrogen peroxide in the presence of ferric ions at the experimental conditions studied.

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Acid Hydrogen Peroxide Treatment of Norway Spruce TMP: The Effect of an Extended pH Range when Catalyzed by Free Ferrous and Free or EDG/EDTA-Chelated Ferric Ions

Journal of Wood Chemistry and Technology ◽

10.1080/02773813.2013.844166 ◽

2013 ◽

Vol 34 (2) ◽

pp. 135-155

Author(s):

Karin Walter ◽

Magnus Paulsson ◽

Per Engstrand

Keyword(s):

Hydrogen Peroxide ◽

Norway Spruce ◽

Ferric Ions ◽

Hydrogen Peroxide Treatment ◽

Ph Range

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Oxidation reduction step in catalytic decomposition of hydrogen peroxide by ferric ions

Transactions of the Faraday Society ◽

10.1039/tf9635902535 ◽

1963 ◽

Vol 59 ◽

pp. 2535 ◽

Cited By ~ 34

Author(s):

Mordechai L. Kremer

Keyword(s):

Hydrogen Peroxide ◽

Catalytic Decomposition ◽

Reduction Step ◽

Ferric Ions ◽

Oxidation Reduction

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STUDIES ON THE ENZYMIC FORMATION OF DI-IODOTYROSINE BY A MICROSOMAL PREPARATION OF GOAT SUBMAXILLARY GLAND

Journal of Endocrinology ◽

10.1677/joe.0.0440177 ◽

1969 ◽

Vol 44 (2) ◽

pp. 177-185 ◽

Cited By ~ 6

Author(s):

RATHA N. HATI ◽

ASOKE G. DATTA

Keyword(s):

Hydrogen Peroxide ◽

Microsomal Fraction ◽

Submaxillary Gland ◽

Maximum Activity ◽

Enzymic Activity ◽

Subcellular Fractions ◽

Ferric Ions ◽

Microsomal Preparation

SUMMARY Subcellular fractions of goat submaxillary gland catalysed the iodination of monoiodotyrosine to form di-iodotyrosine; the microsomal fraction was found to have maximum activity. The enzyme needed copper or hydrogen peroxide for its activity. Thiourea and thiouracil inhibited the enzymic activity. Manganese and ferric ions inhibited the enzymic formation of di-iodotyrosine. The enzyme was solubilized by sodium desoxycholate treatment.

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