Literature DB >> 20440526

Molecular and cellular mechanism of the effect of La(III) on horseradish peroxidase.

Lihong Wang1, Qing Zhou, Tianhong Lu, Xiaolan Ding, Xiaohua Huang.   

Abstract

Horseradish is an important economic crop. It contains horseradish peroxidase (HRP) and lots of nutrients, and has specific pungency. Lanthanum is one of the heavy metals in the environment. It can transfer through the food chain to humans. In this paper, the molecular and cellular mechanism of the toxic effects of La(III) on HRP in vivo was investigated with an optimized combination of biophysical, biochemical, and cytobiological methods. It was found that La(III) could interact with O and/or N atoms in the backbone/side chains of the HRP molecule in the cell membrane of horseradish treated with 80 microM La(III), leading to the formation of a new complex of La and HRP (La-HRP). The formation of the La-HRP complex causes the redistribution of the electron densities of atoms in the HRP molecule, especially the decrease in the electron density of the active center, Fe(III), in the heme group of the La-HRP molecule compared with the native HRP molecule in vivo. Therefore, the electron transfer and the activity of HRP in horseradish treated with 80 microM La(III) are obviously decreased compared with those of the native HRP in vivo. This is a possible molecular and cellular mechanism for the toxic effect of La(III) on HRP in vivo. It is suggested that the accumulation of La in the environment, especially the formation of the La-HRP complex in vivo, is harmful to organisms.

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Year:  2010        PMID: 20440526     DOI: 10.1007/s00775-010-0665-7

Source DB:  PubMed          Journal:  J Biol Inorg Chem        ISSN: 0949-8257            Impact factor:   3.358


  17 in total

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Journal:  Nat Struct Biol       Date:  1997-12

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8.  The critical role of the proximal calcium ion in the structural properties of horseradish peroxidase.

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9.  An Accounting of Horseradish Peroxidase Isozymes Associated with the Cell Wall and Evidence that Peroxidase Does Not Contain Hydroxyproline.

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Journal:  Phytochemistry       Date:  2004-02       Impact factor: 4.072

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