Primary compounds of catalase and peroxidase
- 1 February 1961
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 78 (2) , 253-262
- https://doi.org/10.1042/bj0780253
Abstract
A study has been made of the properties of the primary compound formed between ethyl hydroperoxide and bacterial catalase. The compound is incompletely formed under the experimental conditions and its physical properties have been deduced from an examination of the steady-state reaction mixture. The absorption spectrum obtained for compound I differs from that reported in the literature. It has a very weak Soret band, a band at approximately 360 m[mu] and two bands in the visible at approximately 580 and 660 m[mu]. This spectrum is unlike that of any other iron porphyrin complex. Consideration of the physical and chemical properties of compounds I of bacterial catalase and of peroxidase has led us to suppose that these compounds are mixtures of 2 components. One of the components is a simple ferric t This symbol (t) before abstract number indicates an abstract edited by the editor(s) of the source journal, and republished unaltered by BA editorial staff. porphyrin complex with the hydroperoxide. The other is the result of an attack of the hydroperoxide upon the porphyrin ring.This publication has 17 references indexed in Scilit:
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