Elucidation of the Binding Mechanism of Anionic Phospholipids to Antioxidant Protein Peroxiredoxin 2

Peroxiredoxins (Prxs) belong to a family of ubiquitously expressed peroxidases that detoxify reactive oxygen species. In addition to their enzymatic function, Prxs also function as molecular chaperones. This functional switch is related to their degree of oligomerization. We have previously revealed...

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Bibliographic Details
Published in:	Biochemistry (Easton) Vol. 62; no. 11; pp. 1823 - 1831
Main Authors:	Morita, Kouki, Sasaki, Rino, Jindai, Mami, Yamada, Yutaro, Konno, Hiroki
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 06-06-2023
Subjects:	Antioxidants Molecular Chaperones - metabolism Peroxiredoxins - chemistry Phospholipids Reactive Oxygen Species
Online Access:	Get full text
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Summary:	Peroxiredoxins (Prxs) belong to a family of ubiquitously expressed peroxidases that detoxify reactive oxygen species. In addition to their enzymatic function, Prxs also function as molecular chaperones. This functional switch is related to their degree of oligomerization. We have previously revealed that Prx2 interacts with anionic phospholipids and that the anionic phospholipid-containing Prx2 oligomer forms a high molecular weight (HMW) complex in a nucleotide-dependent manner. However, the detailed mechanism of the oligomer and HMW complex formation remains unclear. In this study, we investigated the anionic phospholipid binding site in Prx2 using site-directed mutagenesis to understand the mechanism of the oligomer formation. Our findings demonstrated that six binding site residues in Prx2 are important for the binding of anionic phospholipids.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0006-2960 1520-4995
DOI:	10.1021/acs.biochem.2c00698