Literature DB >> 3022815

The formation of ES of cytochrome-c peroxidase: a comparison with lactoperoxidase and horseradish peroxidase.

P I Ohlsson, T Yonetani, S Wold.   

Abstract

The activation energy for the formation of the first red compound, ES, for cytochrome-c peroxidase (ferrocytochrome-c: hydrogen-peroxide oxidoreductase, EC 1.11.1.5) by i-propyl hydroperoxide and the rate constants for the formation of ES with various hydroperoxides have been determined. Multivariate data analysis by the partial least-squares model in latent variables has been used to compare the rate constants with the corresponding rate constants for the formation of compound I from lactoperoxidase and two isoenzymes of horseradish peroxidase. The results show that the rate of formation of ES from cytochrome-c peroxidase is highly correlated with the pKa of the hydroperoxides. The activation energy for the formation of ES with i-propyl hydroperoxide is close to the corresponding value for hydrogen peroxide.

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Year:  1986        PMID: 3022815     DOI: 10.1016/0167-4838(86)90113-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Reactivity study on microperoxidase-8.

Authors:  Corrado Dallacosta; Enrico Monzani; Luigi Casella
Journal:  J Biol Inorg Chem       Date:  2003-07-09       Impact factor: 3.358

2.  Catalytic activity, stability, unfolding, and degradation pathways of engineered and reconstituted myoglobins.

Authors:  Raffaella Roncone; Enrico Monzani; Sara Labò; Anna Maria Sanangelantoni; Luigi Casella
Journal:  J Biol Inorg Chem       Date:  2004-11-25       Impact factor: 3.358

  2 in total

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