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PubMed · 3971978

Oxygen binding to dithionite-reduced chloroperoxidase.

A M Lambeir·H B Dunford
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Abstract

Both the kinetics of ferric chloroperoxidase reduction by dithionite and the binding of molecular oxygen to ferrous chloroperoxidase have been studied. The oxyferrous chloroperoxidase decays spontaneously to the ferric enzyme. In addition the corresponding rapid-scan spectra have been recorded. The reduction reaction is caused by SO-.2 with a rate constant of (7.7 +/- 1.0) X 10(4) M-1 S-1. Oxygen binding occurs with a rate constant of (5.5 +/- 1.0) X 10(5) M-1 S-1 over the pH range 3.5-6. Oxyferrous chloroperoxidase has a Soret absorption peak at 428 nm and two partially resolved peaks at 555 nm and 588 nm. Isosbestic points occur at the following wavelengths: between ferrous and oxyferrous chloroperoxidase at 419, 545, 555 and 580 nm; between oxyferrous and ferric chloroperoxidase at 419, 487, 540, 609 and 682 nm.

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Chloride PeroxidaseDithioniteKineticsOxidation-ReductionOxygenPeroxidasesProtein BindingSpectrophotometryJournal ArticleResearch Support, Non-U.S. Gov't

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BibTeXRIS

A M Lambeir, H B Dunford. 1985-02-15. Oxygen binding to dithionite-reduced chloroperoxidase.. https://doi.org/10.1111/j.1432-1033.1985.tb08723.x

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