NDLI: Crystal Structure of Leishmania major Peroxidase and Characterization of the Compound I Tryptophan Radical*

Content Provider	PubMed Central
Author	Jasion, Victoria S. Polanco, Julio A. Meharenna, Yergalem T. Li, Huiying Poulos, Thomas L.
Copyright Year	2011
Abstract	The parasitic protozoa Leishmania major produces a peroxidase (L. major peroxidase; LmP) that exhibits activities characteristic of both yeast cytochrome c peroxidase (CCP) and plant cytosolic ascorbate peroxidase (APX). One common feature is a key Trp residue, Trp208 in LmP and Trp191 in CCP, that is situated adjacent to the proximal His heme ligand in CCP, APX, and LmP. In CCP, Trp191 forms a stable cationic radical after reaction with H2O2 to form Compound I; in APX, the radical is located on the porphyrin ring. In order to clarify the role of Trp208 in LmP and to further probe peroxidase structure-function relationships, we have determined the crystal structure of LmP and have studied the role of Trp208 using electron paramagnetic resonance spectroscopy (EPR), mutagenesis, and enzyme kinetics. Both CCP and LmP have an extended section of β structure near Trp191 and Trp208, respectively, which is absent in APX. This region provides stability to the Trp191 radical in CCP. EPR of LmP Compound I exhibits an intense and stable signal similar to CCP Compound I. In the LmP W208F mutant, this signal disappears, indicating that Trp208 forms a stable cationic radical. In LmP conversion of the Cys197 to Thr significantly weakens the Compound I EPR signal and dramatically lowers enzyme activity. These results further support the view that modulation of the local electrostatic environment controls the stability of the Trp radical in peroxidases. Our results also suggest that the biological role of LmP is to function as a cytochrome c peroxidase.
Related Links	http://dx.doi.org/10.1074/jbc.m111.230524
Ending Page	24615
Page Count	8
Starting Page	24608
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	28
Volume Number	286
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-07-15
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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