Heme destruction, the main molecular event during the peroxide-mediated inactivation of chloroperoxidase from Caldariomyces fumago

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
Marcela AyalaRafael Vazquez-Duhalt

Abstract

Heme peroxidases are subject to a mechanism-based oxidative inactivation. During the catalytic cycle, the heme group is activated to form highly oxidizing species, which may extract electrons from the protein itself. In this work, we analyze changes in residues prone to oxidation owing to their low redox potential during the peroxide-mediated inactivation of chloroperoxidase from Caldariomyces fumago under peroxidasic catalytic conditions. Surprisingly, we found only minor changes in the amino acid content of the fully inactivated enzyme. Our results show that tyrosine residues are not oxidized, whereas all tryptophan residues are partially oxidized in the inactive protein. The data suggest that the main process leading to enzyme inactivation is heme destruction. The molecular characterization of the peroxide-mediated inactivation process could provide specific targets for the protein engineering of this versatile peroxidase.

References

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Citations

Jun 12, 2013·Applied Microbiology and Biotechnology·Milja PešićGregorio Alvaro
Mar 2, 2016·Archives of Biochemistry and Biophysics·Rui ZhangXiaotang Wang
Jul 3, 2013·Vector Borne and Zoonotic Diseases·Ljubo BarbicGiovanni Savini
Oct 17, 2019·Enzyme and Microbial Technology·Flor Sánchez-AlejandroRafael Vazquez-Duhalt

Related Concepts

Cochliobolus
Chloride Peroxidase
High Pressure Liquid Chromatography Procedure
Circular Dichroism, Vibrational
Enzyme Activation
Heme
Oxydol
Oxidation-Reduction
Protein Engineering
Chloride Peroxidase

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